Immunotherapy cells equipped with a collagen-targeting payload

Abstract

The present disclosure relates, in part, to improved therapeutic cells (e.g., comprising immune cells, such as T cells, e.g., human T cells) that encode or express: a collagen-binding payload; and a target-binding protein (e.g., a CAR, a TCR, a scTCR, a TruC, a TCR / CAR, a synNotch receptor, an IFP, or a multispecific T cell engager). In some embodiments, a collagen-binding payload molecule comprises a cytokine, a toxin, a polypeptide that inhibits an interaction between two or more proteins, an antibody or antigen-binding portion thereof, or a combination of any two or more of the foregoing. In certain embodiments, a collagen-binding payload comprises a cytokine (e.g., a human cytokine), such as a proinflammatory cytokine. In some embodiments, the cytokine is an IL-12. In some embodiments (e.g., in a T cell), expression of the collagen-binding payload is driven by binding of NFAT (nuclear factor of activated T cells) to a NFAT binding site (also referred to as NFAT binding motif). In some embodiments, one or more NFAT binding sites are present and can function as a promoter. In some embodiments, an inducible promoter is responsive to NFAT binding to the one or more NFAT binding sites, and the inducible promoter is operably linked to a sequence encoding the collagen-binding payload.

Description

[0001]IMMUNOTHERAPY CELLS EQUIPPED WITH A COLLAGEN-TARGETING PAYLOAD STATEMENT OF GOVERNMENT INTEREST This invention was made with government support under CA225517 awarded by the National Institutes of Health, and W81XWH-21-1-0581 awarded by the U.S. Army Medical Research and Development Command. The government has certain rights in the invention. REFERENCE TO AN ELECTRONIC SEQUENCE LISTING The contents of the electronic sequence listing (360056-513WO-SL.xml; Size: 98,304 bytes; and Date of Creation: May 14, 2025) is herein incorporated by reference in its entirety. BACKGROUND CAR-engineered T (CAR-T) cells and T cell receptor-engineered T (TCR-T) cells are therapeutic approaches to combat cancer cells by providing, e.g., patient-derived T cells with anti-tumor specificity. Although these therapies have shown efficacy against certain blood cancers and in some recent clinical trials, frequent occurrence of therapeutic resistance, especially in solid-tumor settings, means that new improvements are needed. See Baulu, E., Gardet, C., Chuvin, N. & Depil, S. TCR-engineered T cell therapy in solid tumors: State of the art and perspectives. Sci. Adv.9, eadf3700 (2023); Chapuis, A. G. et al. T cell receptor gene therapy targeting WT1 prevents acute myeloid leukemia relapse post-transplant. Nat Med 25, 1064–1072 (2019); Lahman, M. C. et al. Targeting an alternate Wilms’ tumor antigen 1 peptide bypasses immunoproteasome dependency. Sci. Transl. Med.14, eabg8070 (2022); and Bonini, C. et al. Genome Editing in Engineered T Cells for Cancer Immunotherapy. Hum Gene Ther 34, 853–869 (2023). For example, the immunosuppressive tumor microenvironment (TME) causes limited trafficking, infiltration and activation of administered therapeutic T cells and endogenous anti- tumor immune cells. Furthermore, antigen heterogeneity in solid tumors poses additional difficulties for therapeutic T cells, which are designed to recognize specific antigens to lyse cancer cells. A potential approach to boost efficacy of therapeutic T cells involves adding functionality by transducing another gene that expresses a proinflammatory cytokine. IL-12 is a potential candidate due to its high potency to enhance anti-tumor T cell immunity (see Lasek, W., Zagożdżon, R. & Jakobisiak, M. Interleukin 12: still a promising candidate for tumor immunotherapy? Cancer Immunol Immunother 63, 419–435 (2014)). However, uncontrolled activity of IL-12 leads to severe toxicity (see Cohen, J. Clinical trials: IL-12 deaths: explanation and a puzzle. Science 270, 908a–9908 (1995); Leonard, J. P. et al. Effects of single-dose interleukin-12 exposure on interleukin-12-associated toxicity and interferon-gamma production. Blood 90, 2541–2548 (1997); Zhang, L. et al. Tumor-Infiltrating Lymphocytes Genetically Engineered with an Inducible Gene Encoding Interleukin-12 for the Immunotherapy of Metastatic Melanoma. Clinical Cancer Research 21, 2278–2288 (2015)). Zhang et al. isolated tumor-infiltrating lymphocytes (TILs) from melanoma patients, modified the cells to express a single-chain IL-12 fusion (scIL-12) and treated the autologous patients with the T cells (Zhang, L. et al., supra). IL-12 expression was put under control of a nuclear factor of activated T cells (NFAT)-driven promoter, restricting scIL-12 production upon cognate TCR interactions. Although 10 / 16 patients who received > 3e8 T cells had an objective response, 8 / 16 patients exhibited grade > 3 liver toxicity. Approaches to decrease toxicity of IL-12 have been reported. One such strategy is to tether IL-12 on a cell surface; approaches have included fusion of a transmembrane domain (Zhang et al JITC 2019, Hu et al JITC 2021, Lee EHJ et al, Nat Commun 2023), non-covalent cell-surface tethering through fusing an antibody fragment targeting cell surface receptors (Jones 2nd et al, Sci Adv 2022) and conjugation of IL-12-loaded nanoparticles onto azide-labeled CAR- T cells through click chemistry (Luo et al, Biomaterials 2022). These approaches might reduce the chance for IL-12 to act in trans via directly binding to IL-12 receptor on endogenous immune cells; however, these approaches require direct contact between modified T cells and other immune cells for IL-12 to exert functions, which might limit efficacy of IL-12. New modalities are needed for improving cellular immunotherapies. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 shows an example of a lentiviral vector design encoding a Collagen-Binding Domain (CBD)-IL-12 single-chain fusion protein (under control of an inducible (NFAT-driven) minimal promoter) as described herein and a Merkel Cell Carcinoma antigen-specific TCR (TCR “MCC1” (sequences provided herein), under control a constitutive murine stem cell virus (MSCV) promoter). “P2A” = self-cleaving 2A sequence from porcine teschovirus, preceded by an N-terminal GSG linker sequence. A single-chain IL-12 as described herein may be referred to as a “scIL-12” or a “single chain IL-12 variant” or a “single-chain IL-12 fusion protein variant.” Unless expressly indicated otherwise, the IL-12 of a CBD-IL-12 or an IL-12-CBD or a CBD-IL-12-CBD comprises a single-chain IL-12. Figure 2 provides data showing that the lentiviral vector illustrated in Figure 1 can transduce primary human CD8+ T cells to express MCC1 and the CBD-IL-12 fusion protein. The T cells may be referred to as “TCRMCC1.CBD-IL-12” or “MCC1.CBD-IL-12”. Shown from left to right is flow cytometry staining for APC-labeled MCC antigen peptide:HLA tetramers using: untransduced primary human CD8+ T cells, or primary human CD8+ T cells transduced to express: MCC1 alone; MCC1 and a single-chain IL-12; or the MCC1 and the CBD-IL-12 fusion protein. Figure 3 provides data showing that TCRMCC1.NFAT.CBD-IL-12 T cells produce IL-12 and IFN-γ upon coculture with cognate peptide-loaded or unloaded presenter cells. CD8+T cells transduced as described for Figure 2 were cultured overnight with T2 cells loaded with or without cognate peptide antigen. Intracellular IL-12 (y-axis) and IFN-γ (x-axis) were detected the next day by intracellular staining and flow cytometry. Figure 4 shows data from an in vitro killing assay. The graph shows in vitro control of WaGa tumor cells by CD8+ T cells transduced with the indicated construct; untransduced CD8+T cells are included as a comparator. WaGa tumor cell viability was monitored by fluorescence intensity (y-axis). “IL-12” is a single-chain IL-12 fusion protein wherein the p40 and p35 subunits are connected by a linker. “N.CBD-IL-12” = fusion protein wherein a CBD is disposed N-terminal to a single-chain IL-12, as described herein. “C.CBD-IL-12” = fusion protein wherein a CBD is disposed C-terminal to a single-chain IL-12, as described herein. Figures 5A and 5B show results from in vivo studies measuring tumor control and serum IL-12 levels. Briefly, on day -10, 1x107WaGa (HLA-A2+Merkel Cell Polyomavirus (MCPγV)+Merkel Cell Carcinoma (MCC) cell line) cells were injected into a flank of each male, 12-week old NOD scid gamma (NSG) mouse of the study. On day 0, each mouse received an infusion of 5x106human CD4+T cells (transduced to express MCC1, CD8α, and CD8β) and 5x106human CD8+T cells transduced as indicated. (A) Far-left panel: Untransduced CD8+T cells were included as a comparator. Left-center panel: CD8+T cells engineered to express TCR MCC1 under control of a constitutive promoter. Right-center panel: CD8+T cells engineered to express MCC1 under control of a constitutive promoter and a single-chain IL-12 fusion protein variant under control of an NFAT-driven minimal promoter. Far-right panel: CD8+T cells were engineered to express MCC1 under control of a constitutive promoter and a collagen-binding domain (CBD)-scIL-12 fusion protein (CBD fused to N-terminus of scIL-12 p40) under control of the inducible (NFAT-driven) minimal promoter. Tumor volume (average tumor diameter in millimeters (mm)) was measured three times per week and sera was collected as indicated. (B) IL-12 sera concentration at days 3, 7, 10 and 14 days post T cell infusion, in mice administered transduced T cells. Figure 6 relates to in vitro control of tumor cells expressing different antigens by T cells transduced with TCR only, the TCR + CBD-IL-12 fusion protein, or untransduced. Tumor cell viability was monitored by fluorescence intensity (y-axis). Left panel: MAGEA1+A375 melanoma tumor cells were co-cultured with untransduced T cells, MAGEA1-specific TCR- transduced T cells, and MAGEA1-specific TCR + CBD-IL-12 transduced T cells. Center panel: PRAME+H22 lung adenocarcinoma tumor cells were co-cultured with untransduced T cells, PRAME-specific TCR-transduced T cells, and PRAME-specific TCR + CBD-IL-12 transduced T cells. Right panel: WT1+PANC1 pancreatic tumor cells were co-cultured with untransduced T cells, WT1-specific TCR-transduced T cells, and WT1-specific TCR + CBD-IL-12 transduced T cells. Figures 7A-7D relate to certain non-limiting polynucleotide sequences of an example vector of the present disclosure. (A)-(C) show a single polynucleotide sequence, with the sequence starting in (A) and ending in (C). Portions of the sequence underlined are restriction enzyme recognition sites or so-called filler sequences without functional annotations. (D) shows a key describing certain elements of the polynucleotide sequence, with the style of the underlining accompanying each identified element corresponding to the sequence with the same underlining in (A)-(C). Figure 8 provides schematics of certain examples of scIL-12 fusion proteins and data related to certain embodiments of the present disclosure. Left panel: from top to bottom, schematic illustrations of: a scIL-12 fusion protein; a CBD-scIL-12 fusion protein, with a CBD linked to the N-terminus of the IL-12 p40 subunit; a scIL-12-CBD fusion protein, with a CBD linked to the C-terminus of the IL-12 p35 subunit; a CBD-scIL-12-CBD fusion protein, wherein a CBD is linked to the N-terminus of the IL-12 p40 subunit and a CBD is fused to the C- terminus of the IL-12 p35 subunit (while the schematic shows a linker between the CBD and the C-terminus of the IL-12 p35 subunit, see Figure 28E for the amino acid sequence showing direct fusion instead of linkage). Middle panel: The indicated fusion proteins were analyzed by SDS- PAGE under reducing conditions with Coomassie blue staining. Right panel: Dose-response relationship between phosphorylated STAT4 (pY693) and increasing concentrations of the indicated fusion proteins. Figure 9 provides a schematic of certain elements of an example vector of the present disclosure. The illustrated vector is a self-inactivating γ-retroviral vector and was used in the in vitro studies for which results are shown in Figures 10A-10D. In the schematic: “NFAT” = NFAT binding site(s) and an NFAT-binding inducible promoter; “single-chain mIL-12 variant” = one of the fusion protein architectures schematized in the left panel of Figure 8, for these experiments using a single-chain murine IL-12 instead of a single-chain human IL-12; “SFFV” = constitutive SFFV promoter; “hSTEAP1-mBBζ” = chimeric antigen receptor (CAR) comprising an scFv specific for human STEAP1, a transmembrane domain, and murine 4-1BB and CD3ζ intracellular signaling domains; “WPRE” = woodchuck hepatitis virus post- transcriptional regulatory element; “CMV LTR” = long terminal repeat sequence partially deleted and fused to a heterologous promoter sequence of cytomegalovirus; “ΔU3 LTR” = Long terminal repeat with U3 deletion for self-inactivation. Figures 10A-10D show data from experiments characterizing primary murine T cells transduced with a vector according to Figure 9. (A) Expression of the hSTEAP1-mBBζ CAR in murine T cells transduced with a gamma-retroviral vector encoding the CAR alone, the CAR and a single-chain IL-12, the CAR and a CBD-scIL-12 fusion protein, or the CAR and a CBD-scIL- 12-CBD fusion protein. CAR expression was assessed by flow cytometry. Individual values with mean. (B) Percentage lysis (%lysis, y-axis) of unmodified RM9 cells and of RM9 cells transduced to express hSTEAP1 (RM9-hSTEAP1) by primary murine T cells as indicated. Unmodified RM9 or RM9-hSTEAP1 cells were labelled with Calcein-AM dye and co-cultured (24h) with transduced murine T cells at an Effector to Target (E:T) ratio of 1:1 (10,000 T cells / well). Calcein dye released from the target cells was quantified based on fluorescence and % lysis was determined (Mean ± SEM). (C) and (D) Secreted IL-12 (C) and IFNγ (D) by unstimulated and stimulated primary murine T cells (50,000 T cells / well) as described in Figures 10A and 10B. The primary murine T cells were left untreated (no stimulation), or stimulated with RM9 cells, RM9-hSTEAP1 cells, or phorbol 12-myristate 13-acetate and ionomycin (PMA / Iono). The amount (pg / mL) of secreted IL-12 and IFNγ was quantified by an enzyme- linked immunosorbent assay (ELISA). Statistical analyses in Figures (B) and (D) were performed using one-way ANOVA with Tukey’s test (within RM9-hSTEAP1 co-culture samples). **P < 0.01. Figures 11A-11F show results from in vivo studies characterizing CAR-transduced T cells in mice. Briefly, male C57BL6 / J mice received a subcutaneous injection of 5×105RM9- hSTEAP1-firefly luciferase (fluc) cells on day 0. 15 million T cells were administered intravenously on day 4. Biotinylated protein L and Streptavidin Alexa Fluor 647 conjugate were used to determine the percentage of CAR+T cells. T cells transduced with an hSTEAP1-mBBζ CAR construct were 75.3% CAR+. T cells transduced with a hSTEAP1-mBBζ + NFAT-CBD- scIL-12 expression construct were 54.1% CAR+. T cells transduced with a hSTEAP1-mBBζ + NFAT-scIL-12-CBD expression construct were 62.8% CAR+. T cells transduced with a hSTEAP1-mBBζ + NFAT-CBD-scIL-12-CBD expression construct were 52.3% CAR+. (A) Average tumor volumes. (B) Individual tumor growth curves. (C) Survival rates. CR = complete response. (D) Body weight changes normalized to the body weights on day 0 (mean ± SEM). (E) Experimental schedule. (F) Blood samples were collected from tail vein on days 7, 11 and 14. Serum IFN-γ concentrations were quantified by ELISA (mean ± SEM). For the data shown in: Figure 11A (left panel); Figure 11B; and Figure 11C (left panel), UTD, n = 7; hSTEAP1-mBBζ, n = 8. For the data shown in: Figure 11D (right panel); Figure 11E; Figure 11A (right panel); and Figure 11C (right panel), UTD, hSTEAP1-mBBζ + NFAT-CBD-scIL-12 and hSTEAP1-mBBζ + NFAT-CBD-scIL-12-CBD, n = 5; hSTEAP1-mBBζ + NFAT-scIL-12- CBD, n = 6. For the data shown in Figure 11A (left panel) statistical analyses were performed using two-tailed Welch’s t-test. For the data shown in Figure 11C, statistical analyses were performed using log-rank (Mantel-Cox) test. For the data shown in Figure 11F, statistical analyses were performed using Kruskal-Wallis test followed by Dunn’s multiple comparison (non-parametric data). *P < 0.05, **P < 0.01, NS not significant. Figure 12 shows IL-12 levels in tumor, sera, and major organs in mice following administration of scIL-12 fusion protein-equipped CAR-T cells. Briefly, male C57BL6 / J mice received subcutaneous injection of RM9-hSTEAP1 (5×105) on day 0. Five million CAR+ T cells (CAR + NFAT-scIL-12 or CAR + NFAT-CBD-scIL-12 as indicated) were intravenously administered on day 4. Tumors, sera, spleen, and heart were collected on the indicated timepoints. After weighing of tissue samples, IL-12 protein was extracted from tumors and organs by lysis in the presence of protease inhibitors. IL-12 was quantified by ELISA (mean ± SEM). Statistical analyses were performed using two-tailed Welch’s t-test. Left to Right: IL-12 in tumor, serum, spleen, and heart. Figures 13A and 13B show serum levels (in mice) of certain markers of toxicity following administration of untransduced T cells, CAR-T cells, or CAR-T cells expressing an scIL-12 fusion protein (with or without CBD). Briefly, male C57BL6 / J mice received subcutaneous injection of RM9-hSTEAP1 (5×105) on day 0. Ten million CAR+ T cells were intravenously administered on day 4. (A, left to right) Serum CXCL9 concentration on day 11, serum ALT concentration on day 12, serum ALP concentration on day 12. (B, left to right) Intratumoral concentrations of IFN-γ and CXCL9 on day 12. Mean ± SEM. Statistical analyses were performed using one-way ANOVA (A, left and right panels; B, both panels) with Tukey’s test or (A, middle panel) Kruskal-Wallis test followed by Dunn’s multiple comparison (non- parametric data). Figures 14A-14C provide data characterizing hSTEAP1-expressing tumors following administration of the indicated anti-hSTEAP1 CAR-T cells. Briefly, male C57BL6 / J mice received subcutaneous injection of RM9-hSTEAP1 (5×105) on day 0. Five million CAR+ T cells (as indicated) were intravenously administered on day 4. Tumors were collected on day 14 followed by flow cytometric analysis. (A) Tumor volumes (mean ± SEM). (B) Far-left panel: Percentage of CD45+cells within the live cell population. Middle-left panel: Percentage of CD3+CD4-CD8- NK1.1+cells within the live cell population. Center panel: Percentage of CD3+CD4+CD8- NK1.1+cells within the live cell population. Middle-right panel: Percentage of CD3+CD4-CD8+NK1.1+cells within the live cell population. Far-right panel: Percentage of CD62L+CD44+cells within the CD4+T cell population. (C) Far-left panel: Percentage of CD62L+CD44+cells within the CD8+T cell population. Middle-left panel: Percentage of CD103+classical type 1 dendritic cells (cDC1s) within the cDC population. Center panel: Percentage of CD8α+cDC1s within the cDC population. Middle-right panel: Percentage of CD11b+Ly6G+neutrophils within the live cell population. Far-right panel: Percentage of Ly6ChiLy6G- monocytic myeloid-derived suppressor cells (MDSCs) within the live cell population. Statistical analyses were performed using (A, B (left-most and right-most panels), C (left-most panel to center panel, right-most panel), C (right-most panel)) one-way ANOVA with Tukey’s test or (B (second-left to second-right panels), C (second-right panel)) Kruskal-Wallis test followed by Dunn’s multiple comparison (non-parametric data). ****P < 0.0001, NS not significant. Figures 15A-15D provide data from experiments combining CAR-T cells (with or without a scIL-12 fusion protein) with checkpoint inhibitors (anti-PD-1 and anti-CTLA-4 antibodies) to treat established RM9-hSTEAP1 tumor in mice. Briefly, male C57BL6 / J mice received a subcutaneous injection of 5×105RM9-hSTEAP1 cells on day 0. Mice were left untreated or treated with a combination of CAR-T cells and checkpoint inhibitors. Five million CAR+T cells transduced with a vector as indicated were administered intravenously on day 6. Anti-PD1 and anti-CTLA-4 antibodies were administered intraperitoneally on days 9, 13, and 17 at 100 µg each. (A) Tumor volumes were measured (Untreated, n = 3; hSTEAP1-mBBζ, hSTEAP1-mBBζ + NFAT-scIL-12 and hSTEAP1-mBBζ + NFAT-CBD-scIL-12, n = 5. mean ± SEM). (B) Individual tumor growth curves. (C) Percentage survival over time. “CR” = complete response. (D) Left Panel: Percentage initial body weight over time, normalized to body weight measurements taken on day 0 (mean ± SEM). Right Panel: Average tumor volumes in a tumor re-challenge study. Briefly, subjects achieving a CR in the experiment for which data is shown in Figure 15C received a second subcutaneous injection of 5×105RM9-hSTEAP on day 0 of the rechallenge study. Naïve subjects were included as a comparator. Statistical analyses were performed using (C) log-rank (Mantel-Cox) test. *P < 0.05, ** P < 0.01, NS not significant. Figures 16A and 16B provide data showing transduction efficiency of the γ-retroviral vectors for mouse T cells. Primary mouse T cells were analyzed 4 days after transduction. Representative flow cytometric histograms showing (A) CAR (with or without a scIL-12 fusion protein, as indicated) or (B) EGFP expression in primary mouse T cells transduced with gamma- retroviral vectors encoding the indicated transgenes. “UTD” in (A) = untransduced control. Figure 17 shows flow cytometric analysis of human STEAP1 (hSTEAP1) expression in RM9 mouse prostate cancer cell line. RM9 cells were engineered to express hSTEAP1 by gamma-retroviral transduction. The cells were stained with Vandortuzumab (anti-hSTEAP1 human IgG1) followed by anti-human IgG-Alexa Fluor 594. Figures 18A-18C show flow cytometric characteristics of mouse CAR-T cells. (A) Representative flow cytometric pseudo color plots showing the percentage of CD4+ and CD8+ T cells within primary mouse T cells transduced with the indicated CAR (with or without scIL-12 fusion protein, as indicated) vector, or untransduced. (B, C) Representative flow cytometric contour plots showing the expression of CD62L and CD44 in (B) CD8+ and (C) CD4+ cells within primary mouse T cells transduced with the indicated vector, or untransduced. Figure 19 shows individual tumor growth curves corresponding to Figure 11A, right panel. Male C57BL6 / J mice received subcutaneous injection of RM9-hSTEAP1 (5×105) on day 0. Fifteen million T cells (54.1% CAR+ in hSTEAP1-mBBζ + NFAT-CBD-scIL-12, 62.8% CAR+ in hSTEAP1-mBBζ + NFAT-scIL-12-CBD and 52.3% CAR+ in hSTEAP1-mBBζ + NFAT-CBD-scIL-12-CBD) were intravenously administered on day 4. Figure 20 shows detection of IL-12 from tumor and organs. (Left and center panels) Background concentration of IL-12 in major organs from (left panel) untreated, RM9-hSTEAP1 tumor-bearing mice (organs were collected when tumor volume reached the endpoint) or (middle panel) untreated tumor-free mice. (Right panel) IL-12 concentration in lung of RM9-hSTEAP1- bearing mice treated with CAR-T cells also expressing a scIL-12 fusion protein as indicated. N.D., not detected. Figure 21 shows cytokine levels in serum and tumor of mice treated with T cells that were untransduced or that were transduced to express a CAR or a CAR and a scIL-12 fusion protein, as indicated. Male C57BL6 / J mice received subcutaneous injection of RM9-hSTEAP1 (5×105) on day 0.10 million CAR-T cells were intravenously administered on day 4. Serum samples were collected on day 11 for quantification using Legendplex kit. Serum concentrations of (left panel) IFN-γ and (middle panel) TNF-α, and tumor concentration of (right panel) GM- CSF, are shown. Statistical analyses were performed using one-way ANOVA with Tukey’s test. Figure 22 shows percentages of immune cell infiltrates in tumor samples collected from an in vivo study after murine subjects bearing RM9-hSTEAP1 tumors were administered T cells transduced with a vector encoding the indicated CAR or CAR and scIL-12 fusion protein. Far- left panel: Percentage of CD3+cells within the live cell population. Middle-left panel: Percentage of CD3- NK1.1+cells within the live cell population. Middle-right panel: Percentage of CD3+CD4- CD8+NK1.1- cells within the live cell population. Far-right panel: Percentage of CD3+CD4+CD8- NK1.1- cells within the live cell population. Figure 23 shows correlation analyses between RM9-hSTEAP1 tumor volume and frequency of immune cells in mice administered T cells transduced with a vector encoding hSTEAP1-mBBζ CAR, hSTEAP1-mBBζ CAR + NFAT-scIL-12, or hSTEAP1-mBBζ CAR + NFAT-CBD-scIL-12. Figures 24A and 24B show expression levels of PD-1 and CTLA-4 in tumor-infiltrating T and NK cell populations in tumor samples collected from a murine in vivo study. Tumor samples were collected after mice bearing RM9-hSTEAP1 tumor cells were administered T cells transduced with a vector encoding hSTEAP1-mBBζ CAR, hSTEAP1-mBBζ CAR + NFAT- scIL-12, or hSTEAP1-mBBζ CAR + NFAT-CBD-scIL-12. Figures 25A-25C shows tumor volume, serum IFN-γ, and body weight changes in mice with RM9-hSTEAP1 tumor that received anti-hSTEAP1 CAR-T cells (or anti-hSTEAP1 CAR-T cells expressing scIL-12 or CBD-scIL-12 under control of a NFAT promoter) in combination with checkpoint inhibitors. Briefly, male C57BL6 / J mice received subcutaneous injection of RM9-hSTEAP1 (5×105) on day 0. Mice were left untreated or treated with combination immunotherapies of CAR-T cells and CPIs. Five million CAR+ T cells were intravenously administered on day 4.100 µg of anti-PD-1 antibody was administered intraperitoneally on days 7, 11 and 15.100 µg of anti-CTLA-4 antibody was administered on days 7 and 11. (A, left panel) Tumor volumes were measured (Untreated, UTD and hSTEAP1-mBBζ, n = 5; hSTEAP1- mBBζ + NFAT-scIL-12 and hSTEAP1-mBBζ + NFAT-CBD-scIL-12, n = 4. mean ± SEM). (A, right panel) Survival rates. (B) Individual tumor growth curves. (C, left panel) Blood samples were collected from tail vein on days 6, 10, 12 and 16. Serum IFN-γ concentrations were quantified by ELISA (mean ± SEM). (C, right panel) Body weight changes normalized to the body weights on day 0. Statistical analyses were performed using (A, right panel) log-rank (Mantel-Cox) test or (C, left panel) Kruskal-Wallis test followed by Dunn’s multiple comparison. *P < 0.05, ** P < 0.01. CR, complete response. ns, not significant. Figure 26 shows expression of human scIL-12 and human CBD-scIL-12. Recombinant proteins were produced by transient expression in HEK293F cells and analyzed by SDS-page under reducing conditions with Coomassie blue staining. Figure 27 relates to manufacturing of human Jurkat CAR-T cells. Jurkat T cells were analyzed 4 days after transduction. (Left panel) Representative flow cytometric histograms showing CAR expression in Jurkat T cells transduced with gamma-retroviral vectors encoding the indicated transgenes. (Right panel) 50000 CAR+ Jurkat T cells were stimulated with phorbol 12-myristate 13-acetate and ionomycin (PMA / Iono) for 24 h. Secreted IL-12 was quantified by ELISA. Single-chain human IL-12-His and CBD-single-chain human IL-12-His were used to draw standard curves. Figures 28A-28I show amino acid sequences of certain polypeptides of the present disclosure. Figure 28A shows the sequence of an embodiment of a single-chain murine IL-12 fusion protein. The sequence shown includes a C-terminal His-Tag. The fusion protein can be, for example, expressed in a host cell of interest (e.g., HEK293F) and purified using the His-Tag. It will be understood that an alternative tag and / or one or more additional tag, or no tag, may be present. Figure 28B shows the sequence of an embodiment of a single-chain murine IL-12 fusion protein, which can be expressed by a host cell of the present disclosure (e.g., a T cell), optionally along with a target-binding protein such as a CAR, a TCR, a TCR / CAR, a scTCR, a TRuC, a synNotch receptor, a multispecific T cell engager, or an IFP. Figure 28C shows the sequence of an embodiment of a CBD-scIL-12 fusion protein, wherein the scIL-12 is derived from murine IL-12 and the CBD is linked to the N-terminal end of the scIL-12 by a (G3S)2 linker. The fusion protein can be expressed by a host cell of the present disclosure (e.g., a T cell), optionally along with a target-binding protein such as a CAR, a TCR, a TCR / CAR, a scTCR, a TRuC, a synNotch receptor, a multispecific T cell engager, or an IFP. Figure 28D shows the sequence of an embodiment of an scIL-12-CBD fusion protein, wherein the scIL-12 is derived from murine IL-12 and the CBD is directly fused to the C-terminal end of the scIL-12. The fusion protein can be expressed by a host cell of the present disclosure (e.g., a T cell), optionally along with a target-binding protein such as a CAR, a TCR, a TCR / CAR, a scTCR, a TRuC, a synNotch receptor, a multispecific T cell engager, or an IFP. Figure 28E shows the sequence of an embodiment of a CBD-scIL-12-CBD fusion protein, wherein the scIL-12 is derived from murine IL-12, one CBD is linked to the N-terminal end of the scIL-12 by a (G3S)2 linker and one CBD is directly fused to the C-terminal end of the scIL-12. The fusion protein can be expressed by a host cell of the present disclosure (e.g., a T cell), optionally along with a target-binding protein such as a CAR, a TCR, a TCR / CAR, a scTCR, a TRuC, a synNotch receptor, a multispecific T cell engager, or an IFP. Figure 28F shows the sequence of an embodiment of a single-chain human IL-12 fusion protein. The sequence includes a C-terminal His-Tag. The fusion protein can be, for example, expressed in a host cell of interest (e.g., HEK293F) and purified using the His-Tag. It will be understood that an alternative tag and / or one or more additional tag, or no tag, may be present. Figure 28G shows the sequence of an embodiment of a single-chain human IL-12 fusion protein, which can be expressed by a host cell of the present disclosure (e.g., a T cell), optionally along with a target-binding protein such as a CAR, a TCR, a TCR / CAR, a scTCR, a TRuC, a synNotch receptor, a multispecific T cell engager, or an IFP. Figure 28H shows the sequence of an embodiment of a CBD-single-chain human IL-12 fusion protein. The CBD is linked to the N-terminal end of the scIL-12 by a (G3S)2 linker and the sequence includes a C-terminal His-Tag. The fusion protein can be, for example, expressed in a host cell of interest (e.g., HEK293F) and purified using the His-Tag. It will be understood that an alternative tag and / or one or more additional tag, or no tag, may be present. Figure 28I shows the sequence of an embodiment of a CBD-scIL-12 fusion protein, wherein the scIL-12 is derived from human IL-12 and the CBD is linked to the N-terminal end of the scIL-12 by a (G3S)2 linker. The fusion protein can expressed by a host cell of the present disclosure (e.g., a T cell), optionally along with a target-binding protein such as a CAR, a TCR, a TCR / CAR, a scTCR, a TRuC, a synNotch receptor, a multispecific T cell engager, or an IFP. Figure 29 shows a schematic map of an embodiment of a vector of the present disclosure. Due to space constraints, the following features are not displayed: single-chain A3- mIL-12-A3; p35. Figure 30 shows a schematic map of an embodiment of a vector of the present disclosure. Due to space constraints, the following features are not displayed: IgGκ signal peptide; A3; GGGS x 2; GS linker. Figure 31 shows a schematic map of an embodiment of a vector of the present disclosure. Due to space constraints, 18 features are not displayed, including the following: MNDU3 promoter; linker; 4 / 2NQ-2; IgG4 CH3; EGFP-C; UTG-R; promoter mutation; mutated start codon; overlap tga-sffv; sv40 pA-R. Figure 32 shows a schematic map of an embodiment of a vector of the present disclosure. Due to space constraints, the following features are not displayed: promoter mutation; promoter mutation; IgG4-CH3; promoter mutation; NFAT binding site (x8). Figure 33 shows a schematic map of an embodiment of a vector of the present disclosure. Due to space constraints, the following features are not displayed: NFAT binding site (x8). Figure 34 shows an example of a nucleotide sequence comprising an embodiment of a CMV LTR sequence. Underlining corresponds to the sequence features shown in the key at bottom left. Figure 35 shows an example of a nucleotide sequence encoding an anti-STEAP1 chimeric antigen receptor (CAR). The style of underlining in the nucleotide sequence corresponds to the features in the key at the bottom of the figure. From top to bottom, the key features read: SFFV promoter; kozak; GM-CSF signal peptide; scFv VL; GS linker; scFv VH; human IgG4 hinge; 4 / 2NQ = CH2 domain mutations to prevent binding to Fc-gamma receptors; Human IgG4 constant region (CH2 (comprising the 4 / 2NQ sequence) and CH3); Mouse CD28 TM; Mouse 4-1BB; Mouse CD3 zeta. Figure 36 shows an example of a nucleotide sequence encoding an anti-STEAP1 chimeric antigen receptor (CAR). The style of underlining in the nucleotide sequence corresponds to the features in the key at the bottom of the figure. From top to bottom, the key features read: SFFV promoter; kozak; GM-CSF signal peptide; scFv VL; GS linker; scFv VH; human IgG4 hinge; 4 / 2NQ = CH2 domain mutations to prevent binding to Fc-gamma receptors; Human IgG4 constant region (CH2 (comprising the 4 / 2NQ sequence) and CH3); Human CD28 TM; Human 4-1BB; Human CD3 zeta. Figure 37 shows serum IFN-γ levels in mice following administration of CAR T cells expressing an scIL-12 fusion protein (with or without CBD, as indicated). Briefly, C57BL6 / J mice received a subcutaneous injection of RM9-hSTEAP1 cells on day 0. 10 million CAR T cells (CAR + NFAT-scIL-12 or CAR + NFAT-CBD-scIL-12, as indicated) were intravenously injected on day 4 followed by blood sampling on days 7, 10, 11 and 14. Left panel: Experimental timeline. Right Panel: Serum IFN-γ concentrations (pg / mL) were quantified by ELISA. The boxes extend from 25th to 75th percentiles, the center lines show median values, and the whiskers extend to the minimums and maximums. The dotted line shows the detection limit (15.6 pg / mL). Statistical analyses were performed using Mann-Whitney test. P values are shown in the right panel. CBD-scIL-12 CAR-T shows significantly less serum IFN-γ compared with scIL-12- CAR-T cells. Figure 38 shows results from an in vivo study measuring tumor volume and survival curves following administration of anti-hSTEAP1 CAR T cells with (separately administered) CBD-scIL-12 fusion protein (CAR-T + CBD-IL-12 protein) or CAR T cells expressing a CBD- scIL-12 fusion protein under control of a NFAT promoter (CAR + NFAT-CBD-IL-12). Briefly, male C57BL6 / J mice received a subcutaneous injection of RM9-hSTEAP1 cells on day 0. Mice were left untreated or were treated with 5 million CAR T cells intravenously injected on day 4 (CAR or CAR + NFAT-CBD-scIL-12, as indicated) followed by a single intravenous injection of CBD-IL-12 protein on day 8 (10µg or 25µg, as indicated). Top-left panel: Experimental timeline. Bottom-left panel: Average tumor volumes (mean ± SEM). Bottom-right panel: Survival rates. CR = Complete Response. Statistical analyses were performed using log-rank (Mantel-Cox) test. P values are shown in figures. These data show that CBD-scIL-12- CAR T cells outperform the combination therapy of CAR-T cells and CBD-scIL-12 protein therapy. Figure 39 shows results from an in vivo tumor re-challenge study. Briefly, RM9- hSTEAP1 tumor-bearing male C57BL6 / J mice received IL-12-CAR-T cells (CAR + NFAT- scIL-12) or CBD-IL-12-CAR-T cells (CAR + NFAT-CBD-scIL-12) on day 4 after tumor inoculation. Survival curves for complete responders subcutaneously re-challenged with RM9 WT cells (5×105) on day 60 shown. Naïve subjects were included as a comparator. CR = Complete Response. Statistical analyses were performed using log-rank (Mantel-Cox) test. P values are shown in figures. These data show that CBD-scIL-12-hSTEAP1 CAR-T cells induce anti-tumor immune memory to antigens not limited to hSTEAP1. Figure 40 shows results from an in vivo experiment measuring tumor volume and serum IL-12 following administration of anti-hSTEAP1 CAR T cells expressing an scIL-12 fusion protein (with or without CBD) under control of a NFAT promoter. Briefly, male NSG mice received a subcutaneous injection of MyC-CaP-hSTEAP1 cells (5×105) on day 0. Mice were left untreated or were treated with 4 million CAR+T cells (CAR + NFAT-scIL-12 or CAR + NFAT- CBD-scIL-12), derived from male C57BL6 / J mice, intravenously administered on day 8 followed by a blood sampling on day 12 (n = 4 for all groups). Left panel: Experimental Timeline. Center panel: Individual tumor growth curves. Right panel: Serum IL-12 concentrations (pg / mL) were quantified by ELISA (mean ± SEM). Statistical analyses were performed using (center panel) one-way ANOVA with Tukey’s test (on day 16) or (right panel) two-tailed Welch’s t-test. P values are shown in figures. These data show that the addition of a CBD to scIL-12 reduces its systemic circulation in MyC-CaP-hSTEAP1-bearing NSG mice. Figure 41 shows results from an in vivo experiment characterizing CD3+ T cell infiltration of tissue after administration of T cells transduced with CAR, CAR + NFAT-scIL-12, or CAR + NFAT-CBD-scIL-12. Briefly, male C57BL6 / J mice received subcutaneous injection of RM9-hSTEAP1 (5×105) on day 0. 5 million anti-hSTEAP1 CAR-T cells (CAR, CAR + NFAT-scIL-12, or CAR + NFAT-CBD-scIL-12) were intravenously administered on day 4. Immunohistochemistry quantification of CD3+ T cell infiltration in (liver, lung and kidney on day 14 (left, center, and right panels, respectively) is shown. Each data originates from an individual animal. Mean ± SEM is shown. Statistical analyses were performed using (left and center panels) one-way ANOVA with Tukey’s test or (right panel) Kruskal-Wallis test followed by Dunn’s multiple comparison. P values are shown in figures. These data show that the addition of a CBD to scIL-12 decreases IL-12-related toxicity of the CAR-T cells. Figure 42 shows histological analysis of liver, lung, and kidney samples from mice of the in vivo experiment described in Figure 41. Representative H&E and IHC (CD3) staining images are shown. Arrows refer to CD3+ cells; there are more CD3+ cells (indicated by arrows) in H&E images from liver, lung, and kidney of mice that received hSTEAP1-mBBζ+ NFAT-scIL-12 CAR T cells than in corresponding samples of mice that received hSTEAP1-mBBζ CAR T cells or hSTEAP1-mBBζ + NFAT-CBD-scIL-12 CAR T cells. Figures 43A-43G show results of spatial transcriptome analyses of samples collected from an in vivo experiment. Briefly, male C57BL6 / J mice received subcutaneous injection of RM9-hSTEAP1 (5×105) on day 0. 5 million anti-hSTEAP1 CAR-T cells (CAR, CAR + NFAT- scIL-12, or CAR + NFAT-CBD-scIL-12) were intravenously administered on day 4. Tumors were collected on day 14. (A)-(C) Regions of interest (ROI) from hSTEAP1-mBBζ (n=3), hSTEAP1-mBBζ + NFAT-IL-12 (n=4), and hSTEAP1-mBBζ + NFAT-CBD-IL-12 (n=4) treated mice, respectively. Immunofluorescence image depicting pan-cytokeratin (panCK) and CD45 stain as well as representative images of sections stained with H&E and CD3. In the composite image for (A), panCK staining was the dominant staining. In the composite images for (B) and (C), CD45 staining was the dominant staining. (D) Shows a PCA plot showing distribution of selected ROIs based on treatment groups indicated in the key. (E) Shows gene set enrichment analysis showing enriched IL-12 pathway and antigen processing and presentation via MHC- class 1B. (F) and (G) Show heatmaps showing changes in genes involved in pathways as in (E). In general, the Z-scores for the hSTEAP1-mBBζ group were negative. Figures 44A and 44B show further results from the in vivo experiment described in Figures 43A-43E. Male C57BL6 / J mice received subcutaneous injection of RM9-hSTEAP1 (5×105) on day 0.5 million CAR-T cells were intravenously administered on day 4. Tumors were collected on day 14. (A) Tumors were collected for flow cytometric analysis of tumors collected on day 14. Percentage of CD19+B cells within live cells (mean). (B) A heatmap showing transcriptional changes in genes involved in tertiary lymphoid structure. Statistical analysis was performed using (Figure 44A) one-way ANOVA with Tukey’s test. P values are shown in figures. Figures 45A-45C show results from an in vitro experiment characterizing anti-hSTEAP1 CAR-transduced primary human T cells. (A) CAR expression (CAR, CAR + NFAT-scIL-12, or CAR+NFAT-CBD-scIL-12) on expanded primary human T cells was detected on the same day of the functional assays by flow cytometry. The scIL-12 constructs used human IL-12 p40 and p35. (B) Cytokine production upon overnight co-culture of the CAR-transduced primary human T cells with hSTEAP1-positive or hSTEAP1-negative human prostate cancer target cells (22Rv1 cells) was detected with intracellular flow staining. Representative zebra plots from three technical replicates are shown. (C) In vitro killing activity of human CD8 T cells transduced with indicated transgenes against hSTEAP1-positive or hSTEAP1-negative human prostate cancer target cells. Values from three technical replicate (dots) and mean values (lines) are shown. Figures 46A-46E show results from an in vivo experiment testing primary human T cells transduced with CAR, CAR + NFAT-scIL-12, or CAR + NFAT+CBD-scIL-12 in a subcutaneous prostate cancer tumor model in mice. The scIL-12 constructs used components from human IL-12. The CBD was human. The anti-hSTEAP1 CAR comprised human 4-1BB and human CD3ζ signaling domains. (A) Experimental timeline. Briefly, male NSG mice received a subcutaneous injection of 22Rv1-Fluc-RFP (2×106cells) on day 0. 5 million anti- hSTEAP1 CAR+ T cells were intravenously administered on day 13 followed by blood sampling on days 20, 24 and 28 (UTD (control), hSTEAP1-hBBζ, n = 3; hSTEAP1-hBBζ + NFAT-hIL- 12, n = 5; hSTEAP1-hBBζ + NFAT-CBD-hIL-12, n = 4). (B) Average tumor volume (mean ± SEM). Observed complete response (“CR”) rates for hSTEAP1-hBBζ + NFAT-hIL-12 and hSTEAP1-hBBζ + NFAT-CBD-hIL-12 groups on day 50 were 20% and 40%, respectively. Improved (though non-statistically significant) tumor control and overall survival was observed for hSTEAP1-hBBζ + NFAT-CBD-hIL-12 as compared to hSTEAP1-hBBζ + NFAT-hIL-12 groups. (C) Survival curves. An animal in the hSTEAP1-hBBζ + NFAT-hIL-12 group was culled due to graft-versus-host-disease (GVHD) on day 78. (D) Serum IL-12 concentrations were quantified by ELISA (mean). The dotted line shows the detection limit (15.6 pg / mL). (E) Body weight changes normalized to the body weights on day 0 (mean ± SEM). Statistical analyses were performed using (Figure 46C) log-rank (Mantel-Cox) test or (Figure 46D) Two-tailed Welch’s t-test. P values are shown in figures. These data show that primary human CBD-scIL- 12 CAR-T cells show potent therapeutic efficacy and reduce systemic IL-12 in 22Rv1 subcutaneous tumor model. Figures 47A-47D show results from an in vivo tumor control experiment after administration of anti-hSTEAP1 CAR-transduced primary human T cells. (A) Experimental timeline. Briefly, male NSG mice received intravenous injection of 22Rv1-Fluc (1×106) on day - 14. 5 million CAR+ T cells (at a CD4:CD8 ratio of approximately 1:1) were intravenously administered on day 0 (n = 5 for all groups). (B) Serial bioluminescence imaging of NSG mice engrafted with 22Rv1-Fluc metastases and administered T cells as indicated. Radiance scale is shown. (C) Quantification of total flux images overtime. (D) Serum IL-12 concentration on day 12 (mean ± SEM). Statistical analyses were performed using (Figure 47C) one-way ANOVA with Tukey’s test (on day 18) or (Figure 47D) Two-tailed Welch’s t-test. P values are shown in figures. These data show that primary human CBD-scIL-12 CAR-T cells show potent therapeutic efficacy and reduce systemic IL-12 (as compared to CAR-T cells expressing scIL-12 without CBD) in 22Rv1 disseminated metastasis model. Figures 48A-48C show characterization of Jurkat and primary mouse T cells transduced with CAR + NFAT-CBD-scIL-12 or CAR + NFAT-scIL-12-CBD, with EGFP + NFAT-CBD- scIL-12-CBD transduced cells as a comparator. The CAR constructs comprised murine 4-1BB and CD3ζ intracellular signaling domains. The scIL-12 constructs comprised murine IL-12 components. (A) Jurkat cells transduced with EGFP + NFAT-CBD-scIL-12-CBD gamma- retroviral vector were stimulated with PMA / Iono in the presence of Brefeldin A followed by intracellular staining of mouse IL-12. Representative contour plots of n = 2 technical replicates. (B) Primary mouse T cells transduced with the indicated gamma-retroviral vector were stimulated with PMA / Iono in the presence of Brefeldin A followed by intracellular staining of mouse IL-12. Representative contour plots of n = 2 technical replicates. (C) Primary mouse T cells transduced with the indicated gamma-retroviral vector were stimulated with PMA / Iono followed by RNA extraction, reverse transcription and quantitative PCR. Expression levels of mouse p35 and p40 in PMA / Iono stimulated cells relative to unstimulated cells were shown (n = 2 technical replicates). Figures 49A-49I show manufacturing protocols and in vitro characterization of primary human CAR T cells related to Figures 45A-47D and 49D-49I. (A) Experimental timeline for CAR T cells used in Figures 45A-45C, (B) Experimental timeline for CAR T cells used in Figures 46A-46B and Figures 49D-49F, and (C) Experimental timeline for CAR T cells used in Figures 47A-47D and Figures 49G-49I. (D) Representative contour plots of primary human CAR-T cells stained with Biotin-goat anti-Human IgG and PE Streptavidin. (E) Primary human CAR-T cells (50000 CAR-T cells / well) were stimulated with 22Rv1 cells or 22Rv1 hSTEAP1- KO cells for 24 hours. Secreted scIL-12 variants were quantified by ELISA (Mean ± SEM). (F) 22Rv1 cells or 22Rv1 hSTEAP1-KO cells labelled with Calcein-AM were co-cultured with CAR-T cells at the Effector / Target ratio of 1:1 for 24 hours. Calcein released from the target cells was quantified to calculate %target cell lysis (Mean ± SEM). (G) Representative contour plots of primary human CAR-T cells stained with Biotinylated Protein L and PE Streptavidin. CD4+CAR-T cells and CD8+ CAR-T cells were separately analyzed. (H) and (I) Primary human CAR-T cells were co-cultured with 22Rv1 at Effector / Target ratio of 1:2.5. (H) IL-12 secretion from CAR-T cells (Mean ± SEM). (I) Relative cell viability of 22Rv1 target cells over time measured by fluorescence live cell imaging (n = 5 technical replicates, Mean ± SD). Statistical analyses were performed using (Figures 49E and 49F) two-way ANOVA followed by Šídák's multiple comparisons. P values are shown in figures. Figure 50 shows results from in vitro tumor rechallenge experiments. In vitro killing activity of human T cells (transduced with the indicated transgenes) against WaGa cells at an E:T ratio of 5:1. Co-cultures comprised untransduced CD4+ and / or untransduced CD8+ T cells, no CD4 + T cells (ɸ), and / or transduced T cells as indicated. CD8αβ were both wild-type human, and the M1 isoform was used for CD8β. (“2X”) means that double the number of TCR- MCC1-CBD-IL12 CD8+ T cells were used in the absence of CD4+ T cells. This was done to equalize the approximate total T cell number across all groups. Tumor cells were repeatedly added almost every three days. Mean fluorescence intensities for three replicates are shown. These data show that CBD-scIL-12 transduced TCR-MCC1 CD8+ T cells sustain tumor control with the support of TCR-MCC1-CD8αβ-CD200R / CD28 equipped CD4+ T cells. Figure 51 provides data characterizing hSTEAP1-expressing tumors and IFN-γ production from splenic T cells collected from mice following administration of the indicated anti-hSTEAP1 CAR-T cells. Briefly, male C57BL6 / J mice received subcutaneous injection of RM9-hSTEAP1 (5×105) on day 0. CAR+ T cells (as indicated) were intravenously administered on day 4. Tumors were collected on day 14 followed by flow cytometric analysis. Left panel: Percentage of CD8+ T cells within the live cell population. Right panel: Splenic T cells were collected, isolated, and co-cultured with hSTEAP1-positive and negative RM9 prostate cancer cells. “UTD” refers to a co-culture of splenic T cells from a mouse that received untransduced T cells and RM9 cells, as indicated. “hSTEAP1-mBBζ” refers to a co-culture of splenic T cells from a mouse that received anti-STEAP1 CAR T cells (not expressing IL-12), and RM9 cells, as indicated. “hSTEAP1-mBBζ + NFAT-CBD-IL-12” refers to a co-culture of splenic T cells collected from a mouse that received anti-STEAP1 CAR T cells expressing CBD-scIL-12 under control of an NFAT promoter and RM9 cells, as indicated. Figures 52A-52C relate to spatial Transcriptome analysis showing CBD-scIL-12- mediated changes in tumor microenvironment. (A) PCA plot showing distribution of selected regions of interest (ROIs) coded based on treatment groups. (B, C) Heatmaps showing changes in genes involved in pathways in accordance with a gene set enrichment analysis showing enriched IL-12 pathway and antigen processing and presentation via MHC-class 1. Figures 53A-53D relate to studies showing that CAR-T cells expressing a CBD-scIL-12- eradicate established RM9-hSTEAP1 tumor in combination with anti-PD-1 and anti-CTLA-4 checkpoint inhibitors. 5 million CAR+ T cells were intravenously administered on day 6. Anti- PD-1 and anti-CTLA-4 antibodies were administered intraperitoneally 3 times starting at 3 days after the CAR-T administration with 4 days interval. (A) Tumor volumes were measured (Untreated, n = 3; hSTEAP1-mBBζ, hSTEAP1-mBBζ + NFAT-scIL-12 and hSTEAP1-mBBζ + NFAT-CBD-scIL-12, n = 5. mean ± SEM). (B) Survival rates. CR, complete response. (C) Complete responders were subcutaneously re-challenged with RM9-hSTEAP1 cells (5×105) (mean ± SEM). (D) Body weight changes normalized to the body weights on day 0 (mean ± SEM). Statistical analyses were performed using (B) log-rank (Mantel-Cox) test. *P < 0.05, ** P < 0.01, NS not significant. Figure 54 provides data showing that CBD-scIL-12 CAR-T cells remodel immune infiltrates in the tumor. 5 million CAR+ T cells were administered by intravenous injection on Day 4 following Day 0 inoculation with RM9-hSTEAP1 cells. Tumor collection was on day 14. Tumor volumes were measured. Circles = hSTEAP1-mBBζ CAR-T cells. Squares = hSTEAP1- mBBζ + NFAT-scIL-12 CAR-T cells. Triangles = hSTEAP1-mBBζ + NFAT-CBD-scIL-12 CAR-T cells Figure 55 provides data showing that CAR-T-mediated delivery of CBD-scIL-12 demonstrates strong anti-tumor efficacy and induces antigen spreading to counteract antigen heterogeneity in mouse prostate cancer. Survival curves for complete responders subcutaneously rechallenged with RM9 WT cells (5×105) on day 60. Statistics were calculated using the Log- rank (Mantel-Cox) test. DETAILED DESCRIPTION The present disclosure relates, in part, to improved therapeutic cells (e.g., comprising immune cells, such as T cells, e.g., human T cells) that encode or express: a collagen-binding payload; and a target-binding protein. In certain preferred embodiments, the target-binding protein is expressed at a surface of the host cell and the collagen-binding payload is secreted by the host cell. In some embodiments, a collagen-binding payload moiety or molecule comprises a cytokine (optionally, a single-chain fusion protein comprising two or more components of a multicomponent cytokine), a toxin, a polypeptide that inhibits an interaction between two or more proteins, an antibody or antigen-binding portion thereof, or a combination of any two or more of the foregoing. In certain embodiments, a collagen-binding payload comprises a cytokine (e.g., a human cytokine), such as a proinflammatory cytokine. The present disclosure teaches, in part, that expression of a collagen-binding payload, exemplified by a collagen-binding domain in fusion with a cytokine (e.g., CBD-IL-12), by antigen-specific T cells, prevents systemic leakage of the cytokine while the T cells clear tumors in vivo. Moreover, fusion to a collagen-binding domain enhances intratumoral retention of the cytokine. Antigen-specific T cells that express the collagen-binding cytokine fusion have reduced cytokine-related toxicity, maintain anti-tumor inflammatory effects, increase anti-tumor immune infiltrates, demonstrate anti-tumor efficacy without pre-conditioning chemotherapy, and eradicate established tumor in combination with immune checkpoint inhibitors. Furthermore, secreted collagen-binding cytokine fusion demonstrates enhanced localization to tumor and increases cytokine levels in serum and tumor of mice treated with the engineered T cells. In further detail, the present disclosure shows that CAR T cells expressing a collagen- binding cytokine (e.g., a CBD:single-chain IL-12) fusion: outperform therapy comprising separate administration of CAR T cells and the collagen-binding cytokine fusion; induce anti- tumor immunity to antigens not limited to the CAR-recognized antigen(s); provide reduced systemic circulation of the cytokine in mice, as compared to CAR T cells expressing the cytokine without collagen-binding; have decreased cytokine-related toxicity in mice as compared to CAR expressing the cytokine without collagen-binding; and have potent antitumor activity and reduced systemic cytokine levels in a mouse model of disseminated disease; among other advantages. The present disclosure also shows, among other advantages, that TCR T cells expressing a collagen-binding cytokine (e.g., a CBD:single-chain IL-12) fusion outperform TCR T cells not expressing the collagen-binding cytokine fusion in terms of killing tumor cells expressing the antigen recognized by the TCR. The disclosure also shows, among other advantages, that TCR T cells expressing a collagen-binding cytokine (e.g., a CBD:single-chain IL-12) fusion control tumor growth and provide reduced serum cytokine levels as compared to TCR T cells expressing the cytokine without the collagen binding. The present disclosure also shows that, among other advantages, CD8+ TCR T cells expressing a collagen-binding cytokine (e.g., a CBD:single-chain IL-12) fusion effectively control tumor growth when combined with an approximately equivalent number of CD4+ T cells expressing: the TCR, a CD8αβ co-receptor (optionally wherein the CD8β comprises a wild-type or mutant signaling domain from a CD28, as provided herein), and an immunomodulatory fusion protein, optionally comprising: an extracellular portion of a CD200R that is capable of binding to a CD200L, a transmembrane domain or hydrophobic component, and an intracellular wild-type or mutant signaling domain from a CD28, as provided herein; or an extracellular portion of a Fas that is capable of binding to a FasL, a transmembrane domain or hydrophobic component, and an intracellular wild-type or mutant signaling domain from a 4-1BB, as provided herein. A collagen-binding domain (CBD) refers to a polypeptide that binds to collagen, such as human collagen. In some embodiments, a CBD specifically binds to human collagen. A CBD can be from, or be derived from, a native CBD or can be a synthetic (e.g., de novo engineered) polypeptide, A CBD can comprise or can be, for example, a CBD from or derived from: von Willebrand Factor (vWF), such as, for example, a CBD can comprise or can be a vWF A3 domain (e.g., comprising, consisting essentially of, or consisting of the amino acid sequence CSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWN VVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTDVS VDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMVTL GNSFLHKLCSGFVRI (SEQ ID NO.: 5), or the amino acid sequence CSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWN VVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTDVS VDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMVTL GNSFLHKLCSGFVRICTG (SEQ ID NO.: 36), or the amnio acid sequence CSQPLDVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTIDVPWN VVQEKAHLQSLVDLMQQEGGPSQIGDALAFAVRYVTSQIHGARPGASKAVVIIIMDTSL DPVDTAADAARSNRVAVFPVGVGDRYDEAQLRILAGPGASSNVVKLQQVEDLSTMAT LGNSFFHKLCSGFSGV (SEQ ID NO.: 37)) and / or a variant A3 domain comprising one or more of the A3 mutations described in Romijn et al. (J Biol. Chem.276(13):9985-91; doi: 10.1074 / jbc.M006548200) that retain at least partial binding to collagen, a vWF A1 domain (e.g., comprising, consisting essentially of, or consisting of the amino acid sequence or the amino acid sequence CQEPGGLVVPPTDAPVSPTTLYVEDISEPPLHDFYCSRLLDLVFLLDGSSRLSEAEFEVLK AFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQV ASTSEVLKYTLFQIFSKIDRPEASRITLLLMASQEPQRMSRNFVRYVQGLKKKKVIVIPVG IGPHANLKQIRLIEKQAPENKAFVLSSVDELEQQRDEIVSYLC (SEQ ID NO.: 38)), or a vWF fragment or variant thereof that comprises the A3 domain or a variant thereof and / or the A1 domain or a variant thereof, and binds to collagen; a decorin (see, e.g., Svensson et al., J Biol Chem.270(35):201712-6 (1995), doi: 10.1074 / jbc.270.35.20712; e.g. a CBD from a decorin can comprise, consist essentially of, or consist of the amino acid sequence CGPFQQRGLFDFMLEDEASGIGPEVPDDRDFEPSLGPVCPFRCQCHLRVVQCSDLGLDK VPKDLPPDTTLLDLQNNKITEIKDGDFKNLKNLHALILVNNKISKVSPGAFTPLVKLERL YLSKNQLKELPEKMPKTLQELRAHENEITKVRKVTFNGLNQMIVIELGTNPLKSSGIENG AFQGMKKLSYIRIADTNITSIPQGLPPSLTELHLDGNKISRVDAASLKGLNNLAKLGLSFN SISAVDNGSLANTPHLRELHLDNNKLTRVPGGLAEHKYIQVVYLHNNNISVVGSSDFCPP GHNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRSAIQLGNYK (SEQ ID NO.: 39)); a lumican; a fibronectin; a placental growth factor (PlGF), such as PlGF1 or PlGF2 (e.g., comprising, consisting essentially of, or consisting of: the amino acid sequence MPVMRLFPCFLQLLAGLALPAVPPQQWALSAGNGSSEVEVVPFQEVWGRSYCRALERL VDVVSEYPSEVEHMFSPSCVSLLRCTGCCGDENLHCVPVETANVTMQLLKIRSGDRPSY VELTFSQHVRCECRPLREKMKPERRRPKGRGKRRREKQRPTDCHLCGDAVPRR (SEQ ID NO.: 40); and / or the amino acid sequence RRRPKGRGKRRREKQRPTDCHLCGDAVPRR (SEQ ID NO.: 41); and / or the amino acid sequence RRRPKGRGKRRREKQRPTDCHL (SEQ ID NO.: 42); and / or the amino acid sequence RRPKGRGKRRREKQRPTD (SEQ ID NO.: 43); and / or the amino acid sequence RRRPKGRGKRRREKQ (SEQ ID NO.: 44); and / or the amino acid sequence GKRRREKQ (SEQ ID NO.: 45); and / or the amino acid sequence RRRPKGRG (SEQ ID NO.: 46); and / or the amino acid sequence RRKTKGKRKRSRNSQTEEPHP (SEQ ID NO.: 47); a collagen-binding peptide (e.g., comprising, consisting essentially of, or consisting of the amino acid sequence TKKTLRT (SEQ ID NO.: 48), and / or comprising, consisting essentially of, or consisting of the amino acid sequence LRELHLNNN (SEQ ID NO.: 49) (see Katsumata et al., Science Advances 5(11):2019 (doi: 10.1126 / sciadv.aay1971), and / or comprising, consisting essentially of, or consisting of the amino acid sequence WREPFSMALS (SEQ ID NO.: 50) (see Andrades et al., Experimental Cell Research 250(2):485-498 (1999) (doi.org / 10.1006 / excr.1999.4528), and / or comprising, consisting essentially of, or consisting of the amino acid sequence LRELHLNNNC (SEQ ID NO.: 51), and / or comprising, consisting essentially of, or consisting of the amino acid sequence LRELHLDNNC (SEQ ID NO.: 52); a bacterial surface protein (e.g., lipoprotein SLR, M protein, or M-like protein); a collagen mimetic peptide (CMP); an avimer; an antibody or antigen-binding fragment thereof (see, e.g., Liang, H., et al. A collagen-binding EGFR single-chain Fv antibody fragment for the targeted cancer therapy. J Control Release 209, 101-109 (2015); Liang, H., et al. A collagen-binding EGFR antibody fragment targeting tumors with a collagen-rich extracellular matrix. Sci Rep 6, 18205 (2016)); CXCL-12γ (e.g., comprising, consisting essentially of, or consisting of the amino acid sequence KPVSLSYRCPCRFFESHVARANVKHLKILNTPNCALQIVARLKNNNRQVCIDPKLKWIQ EYLEKALNKGRREEKVGKKEKIGKKKRQKKRKAAQKRKN (SEQ ID NO.: 53) and / or the amino acid sequence GRREEKVGKKEKIGKKKRQKKRKAAQKRKN (SEQ ID NO.: 54)); the amino acid sequence set forth in any one or more of SEQ ID NOs.:1-17, 47, and 52 of PCT Publication No. WO 2020 / 0176478, or a polypeptide that has at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity thereto) or a combination of any two or more of the foregoing. These CBDs, and the CBDs described in Liu et al., Front Oncol.13:1225483 (2023), doi: 10.3389 / fonc.2023.1225483), are incorporated herein by reference. In some embodiments, a CBD comprises an amino acid sequence having at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity, or comprises no more than 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 amino acid substitutions, deletions, and / or insertions relative to a parent CBD amino acid sequence (i.e., comprises no more than 1, no more than 2, no more than 3, no more than 4, no more than 5, no more than 6, no more than 7, no more than 8, no more than 9, no more than 10, no more than 11, no more than 12, no more than 13, no more than 14, no more than 15, no more than 16, no more than 17, no more than 18, no more than 19, or no more than 20 amino acid substitutions, deletions, and / or insertions relative to a parent CBD amino acid sequence). It will be appreciated that a CBD of the present disclosure that comprises one or more amino acid substitutions, deletions, and / or insertions relative to a parent (e.g., wild-type CBD) amino acid sequence possesses, and in preferred embodiments at least substantially retains, the ability to bind collagen (e.g., human collagen). In some embodiments, a CBD comprises, consists essentially of, or consists of an amino acid sequence having at least 75%, at least 80%, 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to, and / or comprises no more than 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 amino acid substitutions, deletions, and / or insertions (i.e., no more than 1, no more than 2, no more than 3, no more than 4, no more than 5, no more than 6, no more than 7, no more than 8, no more than 9, no more than 10, no more than 11, no more than 12, no more than 13, no more than 14, no more than 15, no more than 16, no more than 17, no more than 18, no more than 19, or no more than 20 amino acid substitutions, deletions, and / or insertions) relative to, any one or more of the amino acid sequences shown in Table 1: Table 1. Certain CBD amino acid sequences CSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTID VPWNVVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILV TDVSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPT MVTLGNSFLHKLCSGFVRI (SEQ ID NO.: 5); CSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTID VPWNVVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILV TDVSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPT MVTLGNSFLHKLCSGFVRICTG (SEQ ID NO.: 36), or a variant thereof comprising one or more of the A3 mutations described in Romijn et al. (J Biol. Chem.276(13):9985-91; doi: 10.1074 / jbc.M006548200) that retains at least partial binding to collagen; CSQPLDVVLLLDGSSSLPESSFDKMKSFAKAFISKANIGPHLTQVSVIQYGSINTID VPWNVVQEKAHLQSLVDLMQQEGGPSQIGDALAFAVRYVTSQIHGARPGASKAVVIIIM DTSLDPVDTAADAARSNRVAVFPVGVGDRYDEAQLRILAGPGASSNVVKLQQVEDLST MATLGNSFFHKLCSGFSGV (SEQ ID NO.: 37), or a variant thereof comprising one or more of the A3 mutations described in Romijn et al. (J Biol. Chem.276(13):9985-91; doi: 10.1074 / jbc.M006548200) that retains at least partial binding to collagen; CQEPGGLVVPPTDAPVSPTTLYVEDISEPPLHDFYCSRLLDLVFLLDGSSRLSEAE FEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYA GSQVASTSEVLKYTLFQIFSKIDRPEASRITLLLMASQEPQRMSRNFVRYVQGLKKKKVI VIPVGIGPHANLKQIRLIEKQAPENKAFVLSSVDELEQQRDEIVSYLC (SEQ ID NO.: 38); CGPFQQRGLFDFMLEDEASGIGPEVPDDRDFEPSLGPVCPFRCQCHLRVVQCSDL GLDKVPKDLPPDTTLLDLQNNKITEIKDGDFKNLKNLHALILVNNKISKVSPGAFTPLVK LERLYLSKNQLKELPEKMPKTLQELRAHENEITKVRKVTFNGLNQMIVIELGTNPLKSSG IENGAFQGMKKLSYIRIADTNITSIPQGLPPSLTELHLDGNKISRVDAASLKGLNNLAKLG LSFNSISAVDNGSLANTPHLRELHLDNNKLTRVPGGLAEHKYIQVVYLHNNNISVVGSS DFCPPGHNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRSAIQLGNYK (SEQ ID NO.: 39); MPVMRLFPCFLQLLAGLALPAVPPQQWALSAGNGSSEVEVVPFQEVWGRSYCR ALERLVDVVSEYPSEVEHMFSPSCVSLLRCTGCCGDENLHCVPVETANVTMQLLKIRSG DRPSYVELTFSQHVRCECRPLREKMKPERRRPKGRGKRRREKQRPTDCHLCGDAVPRR (SEQ ID NO.: 40); RRRPKGRGKRRREKQRPTDCHLCGDAVPRR (SEQ ID NO.: 41); RRRPKGRGKRRREKQRPTDCHL (SEQ ID NO.: 42); RRPKGRGKRRREKQRPTD (SEQ ID NO.: 43); RRRPKGRGKRRREKQ (SEQ ID NO.: 44); GKRRREKQ (SEQ ID NO.: 45); RRRPKGRG (SEQ ID NO.: 46); RRKTKGKRKRSRNSQTEEPHP (SEQ ID NO.: 47); TKKTLRT (SEQ ID NO.: 48); LRELHLNNN (SEQ ID NO.: 49); WREPFSMALS (SEQ ID NO.: 50); LRELHLNNNC (SEQ ID NO.: 51); LRELHLDNNC (SEQ ID NO.: 52); KPVSLSYRCPCRFFESHVARANVKHLKILNTPNCALQIVARLKNNNRQVCIDPKL KWIQEYLEKALNKGRREEKVGKKEKIGKKKRQKKRKAAQKRKN (SEQ ID NO.: 53); GRREEKVGKKEKIGKKKRQKKRKAAQKRKN (SEQ ID NO.: 54); the amino acid sequence set forth in any one of SEQ ID NOs.:1-17, 47, and 52 of PCT Publication No. WO 2020 / 176478. In some embodiments, a CBD comprises, consists essentially of, or consists of an amino acid sequence having at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to any one or more of the amino acid sequences shown in Table 1. In some embodiments, a CBD comprises, consists essentially of, or consists of an amino acid sequence having at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to an amino acid sequence shown in Table 1. In some embodiments, a CBD comprises, consists essentially of, or consists of an amino acid sequence having at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity to an amino acid sequence shown in Table 1. For use in humans, a CBD preferably comprises, consists essentially of, or consists of an amino acid sequence from a human protein that is capable of binding to human collagen. In some embodiments, a CBD comprises, consists essentially of, or consists of a fully human amino acid sequence. Without being bound by theory, fully human sequences may pose a lower potential for immunogenicity in a human. In some embodiments, a polypeptide of the present disclosure comprises two or more CBD domains (CBDs). In some embodiments, two CBDs (which may be the same or may be different, and if different may be from or derived from different sources; e.g., a CBD from a vWF A3 domain and a CBD from a lumican) may be comprised in a fusion protein, e.g. being linked to or directly fused to one another, and / or being linked or directly fused to a payload such as for example a cytokine. CBDs may be identified by, for example, screening a library of candidate CBDs (e.g., a peptide library, a yeast-display library comprising antibody Fabs, Fvs, Fds, or variable domains, or the like). CBD binding to collagen can be determined using assays known to those having ordinary skill in the art. In some embodiments, binding can be determined using ELISA, surface plasmon resonance (SPR), mass spectrometry, biolayer interferometry (BLI), Western Blot, or the like. For example, Medium binding ELISA microplates (Greiner Bio One) can be coated with 100 μL of 10 μg / mL purified collagen I or III (Sigma-Aldrich) in 1× PBS for 1 h at 37°C. Wells can be subsequently blocked with 200 μL of 2% BSA diluted in in PBS-T (0.5% Tween 20 in 1× PBS) at room temperature for 2 h followed by incubation at room temperature for 1 h with 100 μL serial dilutions of IC in PBSA. Wells can then be incubated for 1 h at room temperature with Peroxidase AffiniPure Goat Anti-Human IgG (H + L) (Jackson ImmunoResearch 115-035- 003; 1:10000) diluted in 100 μL PBSA followed by a 5-10-min room temperature incubation with 100 μL 1-Step Ultra TMB-ELISA Substrate Solution (Thermo Fisher Scientific) in the dark. Reactions can be stopped with 100 μL 1 M sulfuric acid and absorbance at 450 nm, corrected (as needed) with a reference absorbance at 570 nm measured on a BioTek Synergy Mx microplate reader. Three washes can be completed with PBST after each step prior to TMB substrate addition. Equilibrium dissociation constants can be obtained by nonlinear regression analysis assuming one-site specific binding. Experiments can be conducted in duplicate and performed at least three times. As another example, SPR measurements can be carried out with a Biacore X100 instrument. Recombinant human type I or type III collagen (Millipore Sigma) can be immobilized on a CM5 sensor chip by standard amine coupling method (~1500 resonance units (RUs)) and blocked with ethanolamine. A reference cell can also blocked with ethanolamine. Binding assays can be carried out at room temperature and the Kd values can be determined by fitting 1:1 Langmuir binding model to the data using BIAevaluation software (GE Healthcare). As another example, vWF binding to fibrillar human placenta collagen type I (Sigma Chemical Co., St. Louis. MO, cat. no. C-7774) and collagen type III (Sigma, cat. no. C-4407) can be studied in a solid-state binding assay according to Van der Plas et al (Thromb Haemost. 84(6):1005-11 (2000)). Collagen can be coated at 50 μg / ml. A vWF concentration of 2.5 μg / ml can be used. As another example, collagen binding can be assayed by incubating 5 μl of acid- solubilized bovine skin collagen (Vitrogen 100 Collagen, 3 mg / ml, Celtrix Laboratories, Palo Alto, CA) in 0.1 ml of culture medium from cells radiolabeled with [35S]sulfate. After 5 h at 37°C, the sample can be centrifuged for 5 min at 10,000 × g, the supernatant can be removed, and the pellet washed once with phosphate-buffered saline. The pellet and the supernatant can be electrophoresed on a SDS 10% polyacrylamide gel(15), and the amount of [35S]proteoglycan in supernatant and collagen precipitates can be determined in a Bio Imaging Analyzer (Fuji Photo Film Co., Japan). In this analysis only the 35S-labeled proteoglycans corresponding in size to decorin / biglycan may be measured. As another example, ninety-six–well ELISA plates (Greiner Bio-One) can be coated with recombinant collagen (e.g., human type I, type II, type III, or type IV collagen) (Millipore, Sigma); mouse types I and III collagen mixed (Bio-Rad Laboratories); BSA (Sigma-Aldrich), fibronectin (Sigma-Aldrich), fibrinogen (VWF- and fibronectin-depleted; Enzyme Research Laboratories), or elastin (Millipore, Sigma) at 10 μg / ml in PBS overnight at 37°C, then blocked with 2% BSA in 0.05% Tween 20 containing PBS (PBS-T) for 1 hour at room temperature. Then, wells can be washed with PBS-T and further incubated with 15.6 to 1000 nM CBP- conjugated, sequence-scrambled CBP-conjugated, or unmodified antibody for 1 hour at room temperature. After three washes with PBS-T, antibody can be detected by horseradish peroxidase (HRP)–conjugated antibody against rat IgG or mouse IgG and incubated 1 hour at room temperature (Jackson ImmunoResearch). After washes, bound proteins can be detected with tetramethylbenzidine substrate by measurement of the absorbance at 450 nm with subtraction of the absorbance at 570 nm. The apparent KD values can be obtained by nonlinear regression analysis in Prism software (GraphPad Software v8), assuming one site-specific binding. For collagen-binding antibody against human specimens, frozen sections of tendon from a patient with RA and cartilage from a patient with osteoarthritis can be purchased from OriGene Technologies. The sections can be blocked with 2% fetal bovine serum (FBS) in PBS for overnight at room temperature. The sections can be incubated with primary antibodies for 3 hours at room temperature. For tendon sections, either rat α-TNF (50 μg / ml) or equimolar CBP– α-TNF, mouse anti-human CD31 antibody (5 μg / ml; Abcam), and rabbit anti-human type I collagen antibody (5 μg / ml; Abcam) can be used as primary antibodies. For cartilage sections, either rat α-TNF or equimolar CBP–α-TNF (50 μg / ml) and rabbit anti-human type II collagen antibody (5 μg / ml; Abcam) can be used as primary antibodies. After incubating with the fluorescently tagged secondary antibodies, slides can be covered with ProLong Gold Antifade Mountant with 4′,6-diamidino-2-phenylindole (Thermo Fisher Scientific). The images can be scanned with a Pannoramic Digital Slide Scanner (3DHISTECH) and analyzed using Pannoramic Viewer software (3DHISTECH). As another example, affinity of PlGF CBDs can be determined according to the following methodology.96-well ELISA plates can be coated with 10 μg / mL collagen I (EMD Millipore), collagen III (EMD Millipore), or 1 μg / mL recombinant mouse IL-2Ra (SinoBiological) in PBS for 1 hour at 37°C, followed by blocking with 2% BSA in PBS-T for 1 hour at RT. Then, wells can be washed with PBS-T and further incubated with 10 μg / mL CBD- or unmodified IL-2 for 1 hour at RT. After 3 washes with PBS-T, wells can be incubated for 1 hour at RT with biotinylated antibody against IL-2 (eBioscience) and then incubated with HRP-conjugated streptavidin (eBioscience) for 1 hour at RT. After washes, bound CBD-IL-2 and IL-2 can be detected with tetramethylbenzidine substrate by measurement of the absorbance at 450 nm with subtraction of 570 nm. The apparent KD values can be obtained by nonlinear regression analysis in Prism software (v7, GraphPad Software) assuming one-site specific binding. In some embodiments (e.g., in a T cell), expression of the collagen-binding payload is driven by binding of NFAT (nuclear factor of activated T cells) to a NFAT binding site (also referred to as NFAT binding motif). In some embodiments, one or more NFAT binding sites are present and can function as a promoter. In some embodiments, an inducible promoter is responsive to NFAT binding to the one or more NFAT binding sites, and the inducible promoter is operably linked to a sequence encoding the collagen-binding payload. In some embodiments, expression of the collagen-binding payload is driven by binding of NFAT (nuclear factor of activated T cells) to a NFAT binding site (also referred to as NFAT binding motif), optionally to two or more NFAT binding sites, and expression of the target- binding protein is under control of or is driven by a constitutive promoter. In some embodiments, expression of the collagen-binding payload is driven by binding of NFAT (nuclear factor of activated T cells) to a NFAT binding site (also referred to as NFAT binding motif), optionally to two or more NFAT binding sites, and expression of the target- binding protein is under control of or is driven by a SFFV, PGK, EF1-alpha, CAG, MNDU3, CMV, CMV + intron, EFS, CBA, MSCV, MNDU3, SV40, mPGK, hPGK, UBC or CBh promoter. In some embodiments, the payload comprises a cytokine. In some embodiments, the cytokine comprises any one or more of, or is selected from, the following (e.g., human) cytokines: IL-12, IL-1, IL-2, IL-3, IL-4, IL-5, IL-6, IL-7, IL-8, IL-9, IL-10, IL-11, IL-13, IL-14, IL-15, IL-16, IL-17, IL-18, IL-19, IL-20, IL-21, IL-22, IL-23, IL-24, IL-25, IL-26, IL-27, IL-28, IL-29, IL-30, IL-31, IL-32, IL-33, IL-34, IL-35, IL-36, IL-37, IL-38, IL-39, TNF-α, TNF-β, IFNα, IFNβ, IFNγ, CCL1, CCL2, CCL3, CCL4, CCL5, CCL7, CCL8, CCL9, CCL10, CCL11, CCL12, CCL13, CCL14, CCL15, CCL16, CCL17, CCL18, CCL19, CCL20, CCL21, CXCL1, CXCL2 ,CXCL3, CXCL4, CXCL5, CXCL6, CXCL7, CXCL8, CXCL9, CXCL10, CXCL11, CXCL12, CXCL13, CXCL14, CXCL15, CXCL16, CXCL17, GM-CSF, G-CSF, TRAIL, and FASL, or a functional portion or variant thereof. In certain embodiments, a cytokine of the present disclosure has at least 80%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% amino acid sequence identity, similarity, and / or homology to a wild-type human IL-12, IL-1, IL-2, IL-3, IL-4, IL-5, IL-6, IL-7, IL-8, IL-9, IL-10, IL-11, IL-13, IL-14, IL-15, IL-16, IL-17, IL-18, IL-19, IL-20, IL- 21, IL-22, IL-23, IL-24, IL-25, IL-26, IL-27, IL-28, IL-29, IL-30, IL-31, IL-32, IL-33, IL-34, IL- 35, IL-36, IL-37, IL-38, IL-39, TNF-α, TNF-β, IFNα, IFNβ, IFNγ, CCL1, CCL2, CCL3, CCL4, CCL5, CCL7, CCL8, CCL9, CCL10, CCL11, CCL12, CCL13, CCL14, CCL15, CCL16, CCL17, CCL18, CCL19, CCL20, CCL21, CXCL1, CXCL2 ,CXCL3, CXCL4, CXCL5, CXCL6, CXCL7, CXCL8, CXCL9, CXCL10, CXCL11, CXCL12, CXCL13, CXCL14, CXCL15, CXCL16, CXCL17, GM-CSF, G-CSF, TRAIL, or FASL. In certain embodiments, the cytokine comprises (an, e.g., human) IL-12, TNFα, IL-7, CCL4, and / or IFNγ. The present disclosure includes non-limiting examples of CBD:IL-12, CBD:TNFα, CBD:IL-7, CBD:CCL4, and CBD:IFNγ fusion proteins. In some embodiments, a CBD:cytokine fusion comprises, consists essentially of, or consists of: the amino acid sequence shown in: Figure 28G; Figure 28I; SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:2, SEQ ID NO:16, SEQ ID NO:75, SEQ ID NO:77, SEQ ID NO:79, SEQ ID NO:80, SEQ ID NO:82, or SEQ ID NO:18; or the amino acid sequence encoded by SEQ ID NO:24, SEQ ID NO:26, or SEQ ID NO:28. In some embodiments, a target-binding protein is or comprises a TCR comprising a TCRβ chain comprising, consisting essentially of, or consisting of the amino acid sequence shown in SEQ ID NO:85 and a TCRα chain comprising, consisting essentially of, or consisting of the amino acid sequence shown in SEQ ID NO:86. In some embodiments, a target-binding protein is or comprises a CAR comprising, consisting essentially of, or consisting of the amino acid sequence shown in SEQ ID NO:87 or 88. A collagen-binding payload can comprise a fusion protein that comprises a collagen- binding domain (CBD) linked or directly fused to the payload, or to a subunit thereof. A payload can be or comprise, for example, a full-length payload, a payload comprising all subunits thereof, a functional fragment of a parent payload molecule, a functional variant of a parent payload molecule, or any combination thereof. In some embodiments, the payload comprises a cytokine. A cytokine can be or comprise, for example, a full-length cytokine, a cytokine comprising all subunits thereof, a functional fragment of a cytokine, a functional variant of a wild-type cytokine, or any combination thereof. In some embodiments, a cytokine comprises a plurality of subunits and a T cell, host cell, polynucleotide, expression construct, or vector encodes the plurality of subunits. At least one subunit is linked to or directly fused to a CBD. Two or more of the subunits can be provided as a fusion protein, e.g., wherein two subunits are linked via a linker or are directly fused together. Two or more of the subunits can be expressed as separate molecules and can thereafter associate to form, or contribute to the formation of, a cytokine. In some embodiments, a cytokine comprises two subunits and the two subunits are linked via linker or are directly fused together. Accordingly, in some embodiments, all of the subunits of a cytokine are provided as a single-chain fusion protein that further comprises one or more CBD. In some embodiments, less than all of the subunits of a cytokine are provided as a single-chain fusion protein encoded or expressed by the T cell, host cell, polynucleotide, or expression construct and the T cell, host cell, polynucleotide, or expression construct further encodes or expresses the remaining subunit(s). A CBD can be linked or fused directly to the single-chain fusion protein, the remaining subunit(s), if any, or both. In some embodiments, a CBD is from vWF A3 domain and the cytokine is a human IL- 12, such as, for example, a single-chain fusion protein comprising p40 and p35 subunits linked by a linker, and comprising one CBD linked or directly fused to the p40 subunit (e.g., to the N- terminal end thereof), one CBD linked or fused directly to the p35 subunit (e.g., to the C- terminal end thereof), or one CBD linked or directly fused to the p40 subunit (e.g., to the N- terminal end thereof) and one CBD linked or fused directly to the p35 subunit (e.g., to the C- terminal end thereof). It will be understood that the subunits of a cytokine, whether expressed as separate molecules, as a fusion protein, or as a combination of separate molecules and a fusion protein, associate to form a complex that includes one or more CBD and, in certain embodiments, retains at least 20%, at least 30%, at least 40% at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% of one or more function of the parent or wild-type cytokine. In some embodiments, a target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR) that is optionally heterologous to the T cell, a single-chain TCR (scTCR), a TCR / CAR (see PCT application PCT / US2023 / 066466, which published as WO2023215725), a synNotch receptor (see, e.g., PCT application PCT / US2016 / 019188, which published as WO2016138034; see also Allen et al., Science 378:6225 (2022) doi: 10.1126 / science.aba162; and Roybal et al., Cell 164(4):P770-779 (2016), doi org / 10.1016 / j.cell.2016.01.011), a multispecific T cell engager (e.g., a BiTE; e.g., comprising two scFvs, two scFabs, a scFv and a scFab, a scFv and a scTv, a scTv and a scFab, or the like; a multispecific T cell engager can bind to one or more (e.g., tumor) antigen and to: one or more T cell CD3 protein (e.g., CD3ε, CD3γ, or CD3δ, or CD3 complex); and / or a TCR chain; and / or a T cell stimulatory or co-stimulatory protein such as CD28, CD8, CD4, OX40, or 4-1BB), a T cell receptor fusion construct (TRuC), or an immunomodulatory fusion protein (IFP; see, e.g., PCT application PCT / US2016 / 021064, which published as WO2016141357; the IFPs disclosed in U.S. Patent No.12,012,443; PCT application PCT / US2017 / 028693, which published as WO2017184901; the IFPs disclosed in U.S. Pre-Grant Publication 20190127435A1; PCT application PCT / US2018 / 022998, which published as WO2018170475; the IFPs disclosed in U.S. Patent No.11,725,210; PCT application PCT / US2022 / 012609, which published as WO2022155526; the IFPs disclosed in U.S. Pre-Grant Publication 20240076351A1; PCT application PCT / US2023 / 062159, which published as WO2023150801; the IFPs disclosed in U.S. Pre-Grant Publication 2025144211A1; and PCT application PCT / US2022 / 073744, which published as WO2023288281. In some embodiments, a CAR is the CAR of any one of: Tisagenlecleucel, also known as tisa-cel (Kymriah); Axicabtagene ciloleucel, also known as axi-cel (Yescarta); Brexucabtagene autoleucel, also known as brexu-cel (Tecartus); Lisocabtagene maraleucel, also known as liso-cel (Breyanzi); Idecabtagene vicleucel, also known as ide-cel (Abecma); Ciltacabtegene autoleucel, also known as cilta-cel (Carvykti); and C-CAR039. In some embodiments, a TCR, scTCR, or multispecific T cell engager (e.g., comprising (1) a scTv that binds to an antigen:MHC complex and (2) a scFv that binds to a CD3 protein on a T cell) comprises the CDRs and optionally the Vα and Vβ domain amino acid sequences of any of the TCRs disclosed in any of the following documents: PCT / US2012 / 064511, which published as WO 2013 / 071154; PCT / US2015 / 042986, which published as WO 2016 / 022400 (e.g., TCR “C4”; see also the TCRs disclosed in U.S. Patent No.10538572); PCT / US2016 / 068556, which published as WO 2017 / 112944 (see also the TCRs disclosed in U.S. Patent No.11026969); PCT / US2018 / 022759, which published as WO 2018 / 170338 (e.g., TCR “MA-1”; see also the TCRs disclosed in U.S. Patent No.11034748); PCT / US2018 / 046350, which published as WO 2019 / 033057 (e.g., TCR “1”; see also U.S. Pre-Grant Publication No. 20210238250); U.S. Patent No.10,538,574 (e.g., TCR “2”); PCT / US2019 / 03323, which published as WO 2019 / 140278; PCT / US2018 / 063491, which published as WO 2019 / 109047 (see also U.S. Pre-Grant Publication No.20220267403); PCT / US2019 / 017708, which published as WO 2019 / 157524 (e.g., TCR “3”), see also U.S. Pre-Grant Publication No.20200405762; PCT / US2019 / 032527, which published as WO 2019 / 222427, see also U.S. Pre-Grant Publication No.20210252057; PCT / US2020 / 021916, which published as WO 2020 / 185796 (e.g., “TCR 10.1”), see also U.S. Pre-Grant Publication No.20220160764; PCT / US2020 / 018904, which published as WO 2020 / 172332 (see also the TCRs disclosed in U.S. Patent No.11458191); PCT / US2021 / 051840, which published as WO 2022 / 066973 (e.g., TCR “9.3”); PCT / US2019 / 047550, which published as WO 2020 / 041501, see also U.S. Pre-Grant Publication No.20210340201; PCT / US2020 / 047071, which published as WO 2021 / 034976 (e.g., TCR “DL10”), see also U.S. Pre-Grant Publication No.20220409661; PCT / US2019 / 060570, which published as WO 2020 / 097530 (e.g., TCR “Meso-530B11” or TCR “Meso-20B3”), see also U.S. Pre-Grant Publication No.20220009992; PCT / US2021 / 051832, which published as WO 2022 / 066965, see also U.S. Pre-Grant Publication No.20250018036; PCT / US2023 / 066937, which published as WO 2023 / 220718 (e.g., TCR “11N4A” or TCR “11N6”); and PCT / US2023 / 067889, which published as WO 2023 / 235882. In some embodiments, two or more different target-binding proteins are encoded or are expressed. In some embodiments, expression of a target-binding protein is driven by a constitutive promoter. In some embodiments, a constitutive promoter comprises a SFFV, PGK, EF1-alpha, CAG, MNDU3, CMV, CMV + intron, EFS, CBA, MSCV, MNDU3, SV40, mPGK, hPGK, UBC or CBh promoter. In some embodiments, a CAR comprises the CAR amino acid sequence encoded by the polynucleotide sequence shown in Figure 36. In some embodiments, a vector comprises the CMV enhancer, promoter, and LTR elements shown in Figure 34. In some embodiments, a CBD-scIL-12 comprises, consists essentially of, or consists of the amino acid sequence shown in Figure 28I. In some embodiments, a single-chain IL-12 fusion protein comprises, consists essentially of, or consists of the amino acid sequence shown in Figure 28G. In some embodiments, a CBD-scIL-12 comprises a structure as shown in the left-hand panel (lower three schemes) of Figure 8. In some embodiments, a collagen-binding payload comprises a collagen-binding means linked or fused to a payload (e.g., a cytokine or a subunit thereof, a toxin, a polypeptide that inhibits an interaction between two or more proteins, an antibody or antigen-binding portion thereof, or a combination of any two or more of the foregoing. In some embodiments, a collagen-binding payload comprises a collagen-binding polypeptide means linked or fused to a payload (e.g., a cytokine or a subunit thereof, a toxin, a polypeptide that inhibits an interaction between two or more proteins, an antibody or antigen- binding portion thereof, or a combination of any two or more of the foregoing. In certain embodiments, a host cell (e.g., a T cell, such as a human T cell) expresses or encodes (1) a target-binding means and (2) a collagen-binding means linked or fused to a payload. In certain embodiments, a polynucleotide, vector, expression construct, or targeting polynucleotide encodes (1) a target-binding means and (2) a collagen-binding means linked or fused to a payload. Certain embodiments provide a T cell encoding or expressing: (i) a fusion protein that comprises, consists essentially of, or consists of a collagen- binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the T cell encodes or expresses the cytokine; and (ii) a target-binding protein, wherein the target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR) that is optionally heterologous to the T cell, a single-chain TCR (scTCR), a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP). Certain embodiments provide a host cell encoding or expressing a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the host cell encodes or expresses the cytokine, and wherein the host cell comprises a T cell. In some embodiments, the T cell or host cell is a human cell. In some embodiments, the T cell comprises a CD4+ T cell, a CD8+ T cell, a CD4- CD8- double negative T cell, a γδ T cell, a naïve T cell, a central memory T cell, a stem cell memory T cell, an effector memory T cell, or any combination thereof. In some embodiments, the T cell comprises a CD8+ T cell, a CD4+ T cell, or both. Certain embodiments provide a host cell encoding or expressing a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the host cell encodes or expresses the cytokine, and wherein the host cell comprises a human cell. Certain embodiments provide a host cell encoding or expressing a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the host cell encodes or expresses the cytokine, and wherein the host cell comprises a hematopoietic progenitor cell, a stem cell, a peripheral blood mononuclear cell (PBMC), a tumor infiltrating lymphocyte (TIL), or any combination thereof. Certain embodiments provide a host cell encoding or expressing a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the host cell encodes or expresses the cytokine, wherein the host cell comprises an immune system cell, optionally comprising a T cell, a NK cell, a NK-T cell, a dendritic cell, a macrophage, a B cell, a monocyte, or any combination thereof. In some embodiments, the host cell is a human cell. In some embodiments, the host cell further encodes or expresses a target-binding protein, wherein the target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR) that is optionally heterologous to the host cell, a single-chain TCR, a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP). In some embodiments, the target-binding protein is encoded by a polynucleotide or expression construct that also encodes the fusion protein and wherein, optionally, (1) a nucleotide sequence encoding the fusion protein is operably linked to a promoter, wherein, further optionally, (1) the promoter comprises a NFAT binding site and / or is an inducible promoter responsive to NFAT binding to a NFAT binding site and the polynucleotide or expression construct comprises one, two, three, four, five, six, or more NFAT binding sites, one or more of which is operably linked to the inducible promoter, and / or (2) a nucleotide sequence encoding the target-binding protein is operably linked to a constitutive promoter. Expression of a collagen-binding payload (e.g., a CBD-cytokine fusion protein such as, for example, a CBD-scIL-12) can be conditional upon target-recognition by the target-binding protein. Certain embodiments provide a polynucleotide encoding (i) a cytokine, wherein at least a portion (e.g., a subunit) of the cytokine is linked to or is directly fused to a collagen-binding domain (CBD), forming a fusion protein, and (ii) a target-binding protein, wherein the target- binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR), a single- chain TCR, a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP),wherein, optionally: (1) the polynucleotide is codon-optimized for expression in a human T cell; and / or (2) the polynucleotide comprises a promoter operably linked to a nucleotide sequence encoding the target-binding protein, wherein, further optionally, the promoter comprises a constitutive promoter; and / or (3) the polynucleotide comprises a promoter operably linked to a nucleotide sequence encoding the cytokine or a portion thereof, wherein, optionally, the promoter comprises a NFAT binding site and / or is an inducible promoter responsive to NFAT binding to a NFAT binding site and the polynucleotide comprises one, two, three, four, five, six, or more NFAT binding sites, one or more of which is operably linked to the inducible promoter; and / or (4) the cytokine comprises a plurality of subunits, the polynucleotide encodes each of the plurality of subunits, and one or more of the plurality of subunits is linked or is directly fused to one or more CBD, further optionally wherein, between nucleotide sequences encoding the plurality of subunits, are nucleotide sequences that each independently encode a cleavage sequence (e.g., 2A self-cleaving peptide sequence, furin cleavage site) and / or comprise an IRES. Certain embodiments provide an expression construct comprising a promoter operably linked to a nucleotide sequence encoding a fusion protein that comprises, consists essentially of, or consists of: a collagen-binding domain (CBD) linked or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the promoter comprises a NFAT binding site and / or is an inducible promoter operably linked to one or more NFAT binding sites of the expression construct, wherein, optionally, (1) a NFAT-binding site comprises, consists essentially of, or consists of the nucleotide sequence Ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 20), and / or the expression construct comprises two, three, four, five, six, or more NFAT-binding sites, wherein, further optionally, each of the two, three, four, five, six, or more NFAT-binding sites comprises, consists essentially of, or consists of the nucleotide sequence Ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 20), wherein, even further optionally, the expression construct comprises the following nucleotide sequence: Ggaggaaaaactgtttcatacagaaggcgtggaggaaaaactgtttcatacagaaggcgtggaggaaaaactgtttcatacagaaggcgt ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 21), and / or (2) the promoter comprises, consists essentially of, or consists of the nucleotide sequence tagagggtatataatggaagctcgatttccag (SEQ ID NO.: 22); and / or (3) the cytokine comprises a plurality of subunits, the expression vector encodes each of the plurality of subunits, and one or more of the plurality of subunits is linked or is directly fused to one or more CBD, further optionally wherein, between nucleotide sequences encoding the plurality of subunits, are nucleotide sequences that each independently encode a cleavage sequence (e.g., 2A self-cleaving peptide sequence, furin cleavage site, or the like) and / or comprise an IRES; and / or (4) the expression construct further encodes a target-binding protein, wherein the target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR), a single-chain TCR, a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP), wherein a nucleotide sequence encoding the target-binding protein is operably linked to a promoter, wherein, further optionally, the promoter is a constitutive promoter and / or is a SFFV, PGK, EF1-alpha, CAG, MNDU3, CMV, CMV + intron, EFS, CBA, MSCV, MNDU3, SV40, mPGK, hPGK, UBC or CBh promoter. Certain embodiments provide a host cell encoding or expressing a fusion protein comprising (i) a collagen-binding domain (CBD) and (ii) a payload portion, wherein the host cell comprises a human cell, a human immune cell, a tumor infiltrating lymphocyte (TIL), a hematopoietic progenitor cell, a stem cell, a peripheral blood mononuclear cell (PBMC), a T cell, a NK cell, a NK-T cell, a macrophage, a monocyte, a dendritic cell, a B cell, or any combination thereof, and wherein, optionally, the payload portion comprises an antibody or an antigen- binding fragment thereof, a cytokine, a toxin, a polypeptide that inhibits an interaction between two or more proteins, a detectable agent such as a tag or a fluorescent marker, or any combination thereof. Also provided are vectors that comprise a presently disclosed polynucleotide or expression construct. Also provided are targeting polynucleotide constructs comprising a presently disclosed polynucleotide or expression construct, and: a splice acceptor; and / or a sequence encoding a self- cleaving peptide or a cleavage site; and / or a left homology arm homologous to a first portion of a target locus; and / or a polyA sequence; and / or a right homology arm homologous to a second portion of a target locus, wherein, optionally, the target locus comprises safe harbor locus (see, e.g., Pellenz et al., Human Gene Therapy 30(7):814-828 (2019), doi:10.1089 / hum.2018.169), wherein, further optionally, the target locus is or comprises a (e.g., human) TRAC, TRBC, Rosa26, AAVS1, CCR5, CD8α, CD8β, CD4, PDCD1 (PD1), TIGIT, LAG3, BTLA, CTLA4, HAVCR3 (TIM3), TNFRSF18 (GITR), CD47, HLA-A, HLA-B, HLA-C, B2M, or CD40L locus. Also provided is a kit or system comprising: the targeting polynucleotide construct; a guide RNA targeting a portion of the target locus; and a polynucleotide (e.g., mRNA) or vector (e.g., a viral vector) encoding a Cas protein (e.g., Cas9), or a Cas protein and optional amphilphilic peptides for delivery of the Cas protein. Also provided is a host cell comprising a presently disclosed polynucleotide, expression construct, vector, or targeting polynucleotide, wherein, optionally, the host cell comprises a human cell, an immune system cell, a hematopoietic progenitor cell, a stem cell, a peripheral blood mononuclear cell (PBMC), or any combination thereof, wherein, further optionally, the host cell comprises a T cell, a NK cell, a NK-T cell, a dendritic cell, a B cell, a macrophage, a monocyte, or any combination thereof, wherein, even further optionally, the host cell comprises a CD4+ T cell, a CD8+ T cell, a CD4- CD8- double negative T cell, a γδ T cell, a naïve T cell, a central memory T cell, a stem cell memory T cell, an effector memory T cell, a tumor infiltrating lymphocyte (TIL), or any combination thereof. In some embodiments, a host cell CD8+ T cell is provided that encodes or expresses (i) a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the T cell encodes or expresses the cytokine; and (ii) a target-binding protein, wherein the target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR) that is optionally heterologous to the T cell, a single-chain TCR (scTCR), a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP). Host CD8+ T cells can be provided in a composition with, administered with, or administered separately to as a combination cell therapy with CD4+ T cells, for example in about a 1:1 CD8+ to CD4+ ratio. The CD4+ T cells can encode or express: a target-binding protein (optionally, a target-binding protein that binds the same target as the target-binding protein of the CD8+ T cells, and further optionally, is the same target- binding protein as encoded or expressed by the CD8+ T cells); a CD8αβ co-receptor, preferably wherein the CD8β chain is the M1 isoform and / or comprises a wild-type or mutant costimulatory domain from a human CD28 protein, e.g., as provided herein; and an IFP, optionally a CD200R:CD28 IFP or a Fas-4-1BB IFP. In preferred embodiments, the target-binding protein is a TCR, a scTCR, or a TCR-CAR. In some embodiments, a host cell CD8+ T cell is provided that encodes or expresses (i) a fusion protein that comprises, consists essentially of, or consists of a collagen-binding means linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the T cell encodes or expresses the cytokine; and (ii) a target-binding means. Host CD8+ T cells can be provided in a composition with, administered with, or administered separately to as a combination cell therapy with CD4+ T cells, for example in about a 1:1 CD8+ to CD4+ ratio. The CD4+ T cells can encode or express: a target-binding means (optionally, a target-binding means that binds the same target as the target-binding means of the CD8+ T cells, and further optionally, is the same target-binding means as encoded or expressed by the CD8+ T cells); a CD8αβ co-receptor, preferably wherein the CD8β chain is the M1 isoform and / or comprises a wild-type or mutant costimulatory domain from a human CD28 protein, e.g., as provided herein; and an IFP, optionally a CD200R:CD28 IFP or a Fas-4-1BB IFP. In preferred embodiments, the target-binding means is a TCR, a scTCR, or a TCR-CAR. Also provided is a polynucleotide, expression construct, or targeting polynucleotide that encodes: a target-binding protein that is capable of binding a peptide:MHC Class I complex; a CD8αβ co-receptor, preferably wherein the CD8β chain is the M1 isoform and / or comprises a wild-type or mutant costimulatory domain from a human CD28 protein, e.g., as provided herein; and an IFP, optionally a CD200R:CD28 IFP or a Fas-4-1BB IFP. Also provided is a vector that comprises polynucleotide, expression construct, or targeting polynucleotide. Also provided is a(n, e.g., human) CD4+ T cell that comprises the polynucleotide, expression construct, targeting polynucleotide, or vector. Also provided is a(n, e.g., human) CD4+ T cell that expresses: a target-binding protein that is capable of binding a peptide:MHC Class I complex; a CD8αβ co- receptor, preferably wherein the CD8β chain is the M1 isoform and / or comprises a wild-type or mutant costimulatory domain from a human CD28 protein, e.g., as provided herein; and an IFP, optionally a CD200R:CD28 IFP or a Fas-4-1BB IFP. In preferred embodiments, the target- binding protein is a TCR, a scTCR, or a TCR-CAR. In some embodiments, a CD8α comprises, consists essentially of, or consists of the amino acid sequence SQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKA AEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPAKPTTTP APRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVIT LYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV. In some embodiments, an encoded CD8α comprises, consists essentially of, or consists of the amino acid sequence MALPVTALLLPLALLLHAARPSQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQ PRGAAASPTFLLYLSQNKPKAAEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALS NSIMYFSHFVPVFLPAKPTTTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFAC DIYIWAPLAGTCGVLLLSLVITLYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV. In some embodiments, a CD8β comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRR RARLRFMKQFYK. In some embodiments, an encoded CD8β comprises, consists essentially of, or consists of the amino acid sequence MRPRLWLLLAAQLTVLHGNSVLQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQR QAPSSDSHHEFLALWDSAKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIV GSPELTFGKGTQLSVVDFLPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGV LVLLVSLGVAIHLCCRRRRARLRFMKQFYK. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRGGHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIRSKRSRG GHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRGGHSDAMNMTARRAGPTRKHYQAYAAPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRLLHSDAMNMTPRRPGPTRKHYQPYAPPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRLLHSDYMNMTARRAGPTRKHYQPYAPPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRGGHSDAMNMTPRRPGPTRKHYQPYAPPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRGGHSDYMNMTARRAGPTRKHYQPYAPPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRLLHSDAMNMTARRAGPTRKHYQPYAPPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRGGHSDAMNMTARRAGPTRKHYQPYAPPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRLLHSDYMNMTPRRPGPTRKHYQAYAAPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRGGHSDYMNMTPRRPGPTRKHYQAYAAPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRLLHSDAMNMTPRRPGPTRKHYQAYAAPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRLLHSDYMNMTARRAGPTRKHYQAYAAPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRGGHSDAMNMTPRRPGPTRKHYQAYAAPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRGGHSDYMNMTARRAGPTRKHYQAYAAPRDFAAYRS. In some embodiments, a CD8β:CD28 fusion protein comprises, consists essentially of, or consists of the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDS AKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDF LPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRS KRSRLLHSDAMNMTARRAGPTRKHYQAYAAPRDFAAYRS. In any of the presently disclosed embodiments, an encoded CD8β:CD28 fusion protein can comprise, at its N-terminal end, the signal peptide sequence MRPRLWLLLAAQLTVLHGNSV. In some embodiments, a CD8α and a corresponding CD8β, or a CD8α and a corresponding CD8β:CD28, comprise, consist essentially of, or consist of the CD8α and CD8β or CD8β:CD28 (respectively) amino acid sequences (with or without signal peptide) of any one of the following Constructs provided in Table 3 of PCT application US2021063409 (published as WO 2022132836): Construct A; Construct B; Construct E; Construct G. In some embodiments, a CD8α and a corresponding CD8β, or a CD8α and a corresponding CD8β:CD28, comprise, consist essentially of, or consist of the CD8α and CD8β or CD8β:CD28 (respectively) amino acid sequences (with or without signal peptide) of any one of the following Constructs provided in Table 3 of PCT application US2023066048 (published as WO2023212507): Construct BB; Construct CC; Construct DD; Construct EE, Construct FF, Construct GG, Construct HH, Construct II, Construct JJ, Construct KK, Construct LL, Construct MM, Construct NN. In some embodiments, an IFP comprises or consists of the amino acid sequence of an IFP disclosed in PCT application US2016021064 (published as WO2016141357). In some embodiments, an IFP comprises or consists of the amino acid sequence of a CD200R:CD28 IFP disclosed in PCT application US2016021064 (published as WO2016141357). In some embodiments, an IFP comprises or consists of the amino acid sequence of a CD200R:CD28 IFP disclosed in PCT application US2016021064 (published as WO2016141357), with the signal peptide removed. In some embodiments, a CD200R:CD28 IFP, or an encoded CD200R:CD28 IFP comprises, consists essentially of, or consists of any one or more of the following amino acid sequences: MLCPWRTANLGLLLILTIFLVAASSSLCMDEKQITQNYSKVLAEVNTSWPVKMAT NAVLCCPPIALRNLIIITWEIILRGQPSCTKAYRKETNETKETNCTDERITWVSRPDQNSDL QIRPVAITHDGYYRCIMVTPDGNFHRGYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAA QISWIPEGDCATKQEYWSNGTVTVKSTCHWEVHNVSTVTCHVSHLTGNKSLYIELLPVP GAKKSAKLYIPYIILTIIILTIVGFIWLLRSKRSRGGHSDYMNMTPRRPGPTRKHYQPYAPP RDFAAYRS; MDEKQITQNYSKVLAEVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSC TKAYRKETNETKETNCTDERITWVSRPDQNSDLQIRPVAITHDGYYRCIMVTPDGNFHR GYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAAQISWIPEGDCATKQEYWSNGTVTVKS TCHWEVHNVSTVTCHVSHLTGNKSLYIELLPVPGAKKSAKLYIPYIILTIIILTIVGFIWLLR SKRSRGGHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS; MLCPWRTANLGLLLILTIFLVAASSSLCMDEKQITQNYSKVLAEVNTSWPVKMAT NAVLCCPPIALRNLIIITWEIILRGQPSCTKAYRKETNETKETNCTDERITWVSRPDQNSDL QIRPVAITHDGYYRCIMVTPDGNFHRGYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAA QISWIPEGDCATKQEYWSNGTVTVKSTCHWEVHNVSTVTCHVSHLTGNKSLYIELLPVP GAKKSAKL; MDEKQITQNYSKVLAEVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSC TKAYRKETNETKETNCTDERITWVSRPDQNSDLQIRPVAITHDGYYRCIMVTPDGNFHR GYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAAQISWIPEGDCATKQEYWSNGTVTVKS TCHWEVHNVSTVTCHVSHLTGNKSLYIELLPVPGAKKSAKL; YIPYIILTIIILTIVGFIWLL; FWVLVVVGGVLACYSLLVTVAFIIFWV; RSKRSRGGHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS; RSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS; MLCPWRTANLGLLLILTIFLVAASSSLCMDEKQITQNYSKVLAEVNTSWPVKMAT NAVLCCPPIALRNLIIITWEIILRGQPSCTKAYRKETNETKETNCTDERITWVSRPDQNSDL QIRPVAITHDGYYRCIMVTPDGNFHRGYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAA QISWIPEGDCATKQEYWSNGTVTVKSTCHWEVHNVSTVTCHVSHLTGNKSLYIELLPVP GAKKSAKLFWVLVVVGGVLACYSLLVTVAFIIFWVRSKRSRGGHSDYMNMTPRRPGPT RKHYQPYAPPRDFAAYRS; MDEKQITQNYSKVLAEVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSC TKAYRKETNETKETNCTDERITWVSRPDQNSDLQIRPVAITHDGYYRCIMVTPDGNFHR GYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAAQISWIPEGDCATKQEYWSNGTVTVKS TCHWEVHNVSTVTCHVSHLTGNKSLYIELLPVPGAKKSAKLFWVLVVVGGVLACYSLL VTVAFIIFWVRSKRSRGGHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS; MLCPWRTANLGLLLILTIFLVAASSSLCMDEKQITQNYSKVLAEVNTSWPVKMAT NAVLCCPPIALRNLIIITWEIILRGQPSCTKAYRKETNETKETNCTDERITWVSRPDQNSDL QIRPVAITHDGYYRCIMVTPDGNFHRGYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAA QISWIPEGDCATKQEYWSNGTVTVKSTCHWEVHNVSTVTCHVSHLTGNKSLYIELLPVC PSPLFPGPSKPFWVLVVVGGVLACYSLLVTVAFIIFWVRSKRSRGGHSDYMNMTPRRPGP TRKHYQPYAPPRDFAAYRS; MDEKQITQNYSKVLAEVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSC TKAYRKETNETKETNCTDERITWVSRPDQNSDLQIRPVAITHDGYYRCIMVTPDGNFHR GYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAAQISWIPEGDCATKQEYWSNGTVTVKS TCHWEVHNVSTVTCHVSHLTGNKSLYIELLPVCPSPLFPGPSKPFWVLVVVGGVLACYSL LVTVAFIIFWVRSKRSRGGHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS; MLCPWRTANLGLLLILTIFLVAASSSLCMDEKQITQNYSKVLAEVNTSWPVKMAT NAVLCCPPIALRNLIIITWEIILRGQPSCTKAYRKETNETKETNCTDERITWVSRPDQNSDL QIRPVAITHDGYYRCIMVTPDGNFHRGYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAA QISWIPEGDCATKQEYWSNGTVTVKSTCHWEVHNVSTVTCHVSHLTGNKSLYIELLPV; MDEKQITQNYSKVLAEVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSC TKAYRKETNETKETNCTDERITWVSRPDQNSDLQIRPVAITHDGYYRCIMVTPDGNFHR GYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAAQISWIPEGDCATKQEYWSNGTVTVKS TCHWEVHNVSTVTCHVSHLTGNKSLYIELLPV; CPSPLFPGPSKP; MLCPWRTANLGLLLILTIFLVAASSSLCMDEKQITQNYSKVLAEVNTSWPVKMAT NAVLCCPPIALRNLIIITWEIILRGQPSCTKAYRKETNETKETNCTDERITWVSRPDQNSDL QIRPVAITHDGYYRCIMVTPDGNFHRGYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAA QISWIPEGDCATKQEYWSNGTVTVKSTCHWEVHNVSTVTCHVSHLTGNKSLYIELCPSPL FPGPSKPFWVLVVVGGVLACYSLLVTVAFIIFWVRSKRSRGGHSDYMNMTPRRPGPTRK HYQPYAPPRDFAAYRS; MDEKQITQNYSKVLAEVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSC TKAYRKETNETKETNCTDERITWVSRPDQNSDLQIRPVAITHDGYYRCIMVTPDGNFHR GYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAAQISWIPEGDCATKQEYWSNGTVTVKS TCHWEVHNVSTVTCHVSHLTGNKSLYIELCPSPLFPGPSKPFWVLVVVGGVLACYSLLVT VAFIIFWVRSKRSRGGHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS; MLCPWRTANLGLLLILTIFLVAASSSLCMDEKQITQNYSKVLAEVNTSWPVKMAT NAVLCCPPIALRNLIIITWEIILRGQPSCTKAYRKETNETKETNCTDERITWVSRPDQNSDL QIRPVAITHDGYYRCIMVTPDGNFHRGYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAA QISWIPEGDCATKQEYWSNGTVTVKSTCHWEVHNVSTVTCHVSHLTGNKSLYIEL; MDEKQITQNYSKVLAEVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSC TKAYRKETNETKETNCTDERITWVSRPDQNSDLQIRPVAITHDGYYRCIMVTPDGNFHR GYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAAQISWIPEGDCATKQEYWSNGTVTVKS TCHWEVHNVSTVTCHVSHLTGNKSLYIEL. In some embodiments, an IFP comprises or consists of the amino acid sequence of an IFP disclosed in PCT application US2018022998 (published as WO2018170475). In some embodiments, an IFP comprises or consists of the amino acid sequence of a Fas:4-1BB IFP disclosed in PCT application US2018022998 (published as WO2018170475). In some embodiments, an IFP comprises or consists of the amino acid sequence of a Fas:4-1BB IFP disclosed in PCT application US2018022998 (published as WO2018170475), with the signal peptide removed. In some embodiments, an IFP comprises or consists of the amino acid sequence of SEQ ID NO:188 or 186 in PCT application US2018022998 (published as WO2018170475), with the signal peptide removed. In some embodiments, an IFP comprises or consists of the amino acid sequence of SEQ ID NO:188 or 186 in PCT application US2018022998 (published as WO2018170475). In some embodiments, a Fas:4-1BB IFP, or an encoded Fas:4-1BB IFP comprises, consists essentially of, or consists of any one or more of the following amino acid sequences: MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHD GQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGL EVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSN; QVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDE PDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNST VCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSN; MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHD GQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGL EVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCK; QVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDE PDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNST VCEHCDPCTKCEHGIIKECTLTSNTKCK; MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHD GQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGL EVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTS; QVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDE PDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNST VCEHCDPCTKCEHGIIKECTLTS; LGWLCLLLLPIPLIVWV; IISFFLALTSTALLFLLFFLTLRFSVV; MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHD GQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGL EVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNL GWLCLLLLPIPLIVWVKRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEEGGCEL; QVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDE PDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNST VCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNLGWLCLLLLPIPLIVWVKRGRKKLL YIFKQPFMRPVQTTQEEDGCSCRFPEEEEGGCEL; MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHD GQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGL EVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNII SFFLALTSTALLFLLFFLTLRFSVVKRGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEE GGCEL; QVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDE PDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNST VCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNIISFFLALTSTALLFLLFFLTLRFSVVK RGRKKLLYIFKQPFMRPVQTTQEEDGCSCRFPEEEEGGCEL. In some embodiments: the CD8α comprises the amino acid sequence SQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKA AEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPAKPTTTP APRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVIT LYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV; the CD8β comprises the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDSAKGTI HGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDFLPTTA QPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRRARLR FMKQFYK; and the IFP is a CD200R:CD28 IFP. In some embodiments: a CD8α comprises the amino acid sequence SQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKA AEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPAKPTTTP APRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVIT LYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV; a CD8β comprises the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDSAKGTI HGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDFLPTTA QPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRRARLR FMKQFYK; and the IFP is a Fas:4-1BB IFP. In some embodiments: a CD8α comprises the amino acid sequence SQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKA AEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPAKPTTTP APRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVIT LYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV; a CD8β:CD28 fusion comprises the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDSAKGTI HGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDFLPTTA QPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRSKRSR LLHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS; and the IFP is a CD200R:CD28 IFP. In some embodiments: a CD8α comprises the amino acid sequence SQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKA AEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPAKPTTTP APRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVIT LYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV; a CD8β:CD28 fusion comprises the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDSAKGTI HGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDFLPTTA QPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRSKRSR LLHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS; and the IFP is a Fas:4-1BB IFP. In some embodiments: a CD8α comprises the amino acid sequence SQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKA AEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPAKPTTTP APRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVIT LYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV; a CD8β:CD28 fusion comprises the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDSAKGTI HGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDFLPTTA QPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRSKRSR GGHSDAMNMTARRAGPTRKHYQAYAAPRDFAAYRS; and the IFP is a CD200R:CD28 IFP. In some embodiments: a CD8α comprises the amino acid sequence SQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKA AEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPAKPTTTP APRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVIT LYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV; a CD8β:CD28 fusion comprises the amino acid sequence LQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDSAKGTI HGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDFLPTTA QPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRSKRSR GGHSDAMNMTARRAGPTRKHYQAYAAPRDFAAYRS; and the IFP is a Fas:4-1BB IFP. Also provided is a cell population or composition comprising a plurality of a presently disclosed T and / or a plurality of a presently disclosed host cell. Also provided is a composition comprising: (1) a T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, cell population, or composition as disclosed herein; and (2) a pharmaceutically acceptable carrier, excipient, or diluent. Also provided is a method comprising introducing into a host cell a presently disclosed polynucleotide, expression construct, vector, targeting polynucleotide construct, or composition. Also provided is a host cell made by the method. Also provided are methods and uses of a presently disclosed T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, cell population, or composition, in treating a disease or disorder, such as, for example, a cancer. In some embodiments, the cancer comprises a solid tumor. In some embodiments, the cancer comprises a hematological malignancy. In some embodiments, the cancer comprises prostate cancer. In some embodiments, the cancer comprises metastatic castration-resistant prostate cancer (mCRPC). In some embodiments, the cancer comprises pancreatic cancer. In some embodiments, the cancer comprises breast cancer. Prior to setting forth this disclosure in more detail, it may be helpful to an understanding thereof to provide definitions of certain terms to be used herein. Additional definitions are set forth throughout this disclosure. In the present description, any concentration range, percentage range, ratio range, or integer range is to be understood to include the value of any integer within the recited range and, when appropriate, fractions thereof (such as one tenth and one hundredth of an integer), unless otherwise indicated. Also, any number range recited herein relating to any physical feature, such as polymer subunits, size or thickness, are to be understood to include any integer within the recited range, unless otherwise indicated. As used herein, the term "about" means ± 20% of the indicated range, value, or structure, unless otherwise indicated. It should be understood that the terms "a" and "an" as used herein refer to "one or more" of the enumerated components. The use of the alternative (e.g., "or") should be understood to mean either one, both, or any combination thereof of the alternatives. As used herein, the terms "include", "have", and "comprise" are used synonymously, which terms and variants thereof are intended to be construed as non-limiting. In addition, it should be understood that the individual compounds, or groups of compounds, derived from the various combinations of the structures and substituents described herein, are disclosed by the present application to the same extent as if each compound or group of compounds was set forth individually. Thus, selection of particular structures or particular substituents is within the scope of the present disclosure. The term "consisting essentially of" is not equivalent to "comprising" and refers to the specified materials or steps of a claim, or to those that do not materially affect the basic characteristics of a claimed subject matter. For example, a protein domain，region, or module (e.g., a binding domain, hinge region, linker module) or a protein (which may have one or more domains, regions, or modules) "consists essentially of" a particular amino acid sequence when the amino acid sequence of a domain, region, module, or protein includes extensions, deletions, mutations, or a combination thereof (e.g., amino acids at the amino- or carboxy-terminus or between domains) that, in combination, contribute to at most 20% (e.g., at most 15%, at most 10%, at most 8%, at most 6%, at most 5%, at most 4%, at most 3%, at most 2% or at most 1% ) of the length of a domain, region, module, or protein and do not substantially affect (i.e., do not reduce the activity by more than 50%, such as no more than 40%, no more than 30%, no more than 25%, no more than 20%, no more than 15%, no more than 10%, no more than 5%, or no more than 1% ) the activity of the domain(s), region(s), module(s), or protein (e.g., the target binding affinity or avidity of a binding protein). As used herein, "protein" or "polypeptide" refers to a polymer of amino acid residues. Proteins apply to naturally occurring amino acid polymers, as well as to amino acid polymers in which one or more amino acid residue is an artificial chemical mimetic of a corresponding naturally occurring amino acid and non-naturally occurring amino acid polymers. In some embodiments, a "peptide" (e.g., a peptide antigen) refers to a polymer of about 8-10 amino acid residues in length. It will be understood that a polypeptide multimer (e.g., a TCR) may be referred to as a “protein.” As used herein, a "hematopoietic progenitor cell" is a cell that can be derived from hematopoietic stem cells or fetal tissue and is capable of further differentiation into mature cell types (e.g., immune system cells). Exemplary hematopoietic progenitor cells include those with a CD24Lo Lin– CD117+ phenotype or those found in the thymus (referred to as progenitor thymocytes). As used herein, an "immune system cell" or “immune cell” means any cell of the immune system that originates from a hematopoietic stem cell in the bone marrow, which gives rise to two major lineages, a myeloid progenitor cell (which give rise to myeloid cells such as monocytes, macrophages, dendritic cells, megakaryocytes and granulocytes) and a lymphoid progenitor cell (which give rise to lymphoid cells such as T cells, B cells and natural killer (NK) cells). Exemplary immune system cells include a CD4+ T cell, a CD8+ T cell, a CD4- CD8- double negative T cell, a γδ T cell, a regulatory T cell, a natural killer cell, a natural killer T cell, and a dendritic cell. Macrophages and dendritic cells can be referred to as "antigen presenting cells" or "APCs," which are specialized cells that can activate T cells when a major histocompatibility complex (MHC) receptor on the surface of the APC complexed with a peptide interacts with a TCR on the surface of a T cell. A "T cell" or "T lymphocyte" is an immune system cell that matures in the thymus and produces a T cell receptor (TCR), though it will be understood that a T cell which has been modified to prevent production of a TCR by the T cell (e.g., by introduction of an inhibitory oligonucleotide or genetic modification to prevent production of a TCR) is still considered to be a T cell. T cells can be naïve ("TN"; not exposed to antigen; increased expression of CD62L, CCR7, CD28, CD3, CD127, and CD45RA, and decreased or no expression of CD45RO as compared to TCM (described herein)), memory T cells (TM) (antigen experienced and long- lived), including stem cell memory T cells, and effector cells (antigen-experienced, cytotoxic). TM can be further divided into subsets of central memory T cells (TCM, expresses CD62L, CCR7, CD28, CD95, CD45RO, and CD127) and effector memory T cells (TEM, express CD45RO, decreased expression of CD62L, CCR7, CD28, and CD45RA). Effector T cells (TE) refers to antigen-experienced CD8+ cytotoxic T lymphocytes that express CD45RA, have decreased expression of CD62L, CCR7, and CD28 as compared to TCM, and are positive for granzyme and perforin. Helper T cells (TH) are CD4+ cells that influence the activity of other immune cells by releasing cytokines. CD4+ T cells can activate and suppress an adaptive immune response, and which of those two functions is induced will depend on presence of other cells and signals. T cells can be collected using known techniques, and the various subpopulations or combinations thereof can be enriched or depleted by known techniques, such as by affinity binding to antibodies, flow cytometry, or immunomagnetic selection. Other exemplary T cells include regulatory T cells, such as CD4+ CD25+ (Foxp3+) regulatory T cells and Treg17 cells, as well as Tr1, Th3, CD8+CD28-, and Qa-1 restricted T cells. "T cell receptor" (TCR) refers to an immunoglobulin superfamily member having a variable binding domain, a constant domain, a transmembrane region, and a short cytoplasmic tail; see, e. g., Janeway et al., Immunobiology: The Immune System in Health and Disease, 3rd Ed., Current Biology Publications, p.433, 1997) capable of specifically binding to an antigen peptide bound to a MHC receptor. A TCR can be found on the surface of a cell or in soluble form and generally is comprised of a heterodimer having α and β chains (also known as TCR α and TCRβ, respectively), or γ and δ chains (also known as TCRγ and TCRδ, respectively). In certain embodiments, a polynucleotide encoding a binding protein of this disclosure, e.g., a TCR, can be codon optimized to enhance expression in a particular host cell, such, for example, as a cell of the immune system, a hematopoietic stem cell, an embryonic stem cell, a T cell, a primary T cell, a T cell line, a NK cell, or a natural killer T cell (Scholten et al., Clin. Immunol.119:135, 2006). Exemplary T cells that can express binding proteins and TCRs of this disclosure include CD4+ T cells, CD8+ T cells, and related subpopulations thereof (e.g., naïve, central memory, stem cell memory, effector memory). Like other immunoglobulins (e.g., antibodies), the extracellular portion of TCR chains (e.g., α-chain, β-chain) can contain two immunoglobulin domains, a variable domain (e.g., α- chain variable domain or Vα, β-chain variable domain or Vβ at the N-terminus, and one constant domain (e.g., α-chain constant domain or Cα, β-chain constant domain or Cβ) adjacent the cell membrane. Also, like antibodies, the variable domains contain complementary determining regions (CDRs) separated by framework regions (FRs) (see, e.g., Jores et al., Proc. Nat'l Acad. Sci. USA 87:9138, 1990; Chothia et al., EMBO J.7:3745, 1988; see also Lefranc et al., Dev. Comp. Immunol.27:55, 2003). The source of a TCR as used in the present disclosure may be from various animal species, such as a human, mouse, rat, rabbit, or other mammal. The term "variable region" or "variable domain" refers to the domain of an immunoglobulin superfamily binding protein (e.g., a TCR α-chain or β-chain (or γ chain and δ chain for γδ TCRs)) that is involved in binding of the immunoglobulin superfamily binding protein (e.g., TCR) to antigen. The variable domains of the α chain and β chain (Vα and Vβ, respectively) of a native TCR generally have similar structures, with each domain comprising four generally conserved framework regions (FRs) and three CDRs. The Vα domain is encoded by two separate DNA segments, the variable gene segment, and the joining gene segment (V-J); the Vβ domain is encoded by three separate DNA segments, the variable gene segment, the diversity gene segment, and the joining gene segment (V-D-J). A single Vα or Vβ domain may be sufficient to confer antigen-binding specificity. Furthermore, TCRs that bind a particular antigen may be isolated using a Vα or Vβ domain from a TCR that binds the antigen to screen a library of complementary Vα or Vβ domains, respectively. The terms "complementarity determining region" and "CDR" are synonymous with "hypervariable region" or "HVR," and are known in the art to refer to sequences of amino acids within immunoglobulin (e.g., TCR) variable regions. CDRs confer antigen specificity and binding affinity and are separated from one another in primary amino acid sequence by framework regions. In general, there are three CDRs in each TCR α-chain variable region (αCDR1, αCDR2, αCDR3) and three CDRs in each TCR β-chain variable region (βCDR1, βCDR2, βCDR3). In TCRs, CDR3 is thought to be the main CDR responsible for recognizing processed antigen (see e.g., Rosati et al. BMC Biotechnology 201717:61 (describing an essential role for CDR3 in the interaction of the TCR with the peptide-MHC complex) and Fischer et al. Mol Syst Bio.16:e9416 (2020) (describing CDR3α and β are "most commonly aligned" with the presented epitope)). In general, CDR1 and CDR2 interact mainly or exclusively with the MHC. CDR1 and CDR2 are encoded within the variable gene segment of a TCR variable region-coding sequence, whereas CDR3 is encoded by the region spanning the variable and joining segments for Vα, or the region spanning variable, diversity, and joining segments for Vβ. Thus, if the identity of the variable gene segment of a Vα or Vβ is known, the sequences of their corresponding CDR1 and CDR2 can be deduced; e.g., according to a numbering scheme as described herein. Compared with CDR1 and CDR2, CDR3, and in particular CDR3β, is typically significantly more diverse due to the addition and loss of nucleotides during the recombination process. TCR variable domain sequences can be aligned to a numbering scheme (e.g., IMGT, Kabat, Chothia, EU, Enhanced Chothia, or Aho, or a hybrid of two or more of these), allowing equivalent residue positions to be annotated and for different molecules to be compared using, for example, ANARCI software tool (2016, Bioinformatics 15:298-300). A numbering scheme provides a standardized delineation of framework regions and CDRs in the TCR variable domains. In certain embodiments, a CDR of the present disclosure is identified according to the IMGT numbering scheme (Lefranc et al., Dev. Comp. Immunol.27:55, 2003; imgt.org / IMGTindex / V-QUEST.php). In some embodiments, a CDR3 is defined in accordance with the IMGT junction definition (including CYS 104 and PHE 118 or TRP 118). In some embodiments, a CDR3 is defined in accordance with the IMGT definition (rearranged CDR3 corresponding to IMGT positions 105-117 within the variable domain). In some embodiments, a CDR (or all six CDRs of a binding protein) of the present disclosure is identified or defined according to the IMGT numbering scheme. In certain embodiments, a CDR3 (or both CDR3s of a binding protein) is identified or defined according to the IMGT-junction numbering scheme. In some embodiments, a CDR (or all six CDRs of a binding protein) of the present disclosure is identified or defined according to the Kabat numbering scheme. In some embodiments, a CDR (or all six CDRs of a binding protein) of the present disclosure is identified or defined according to the Chothia numbering scheme. In some embodiments, a CDR (or all six CDRs of a binding protein) of the present disclosure is identified or defined according to the EU numbering scheme. In some embodiments, a CDR (or all six CDRs of a binding protein) of the present disclosure is identified or defined according to the Enhanced Chothia numbering scheme. In some embodiments, a CDR (or all six CDRs of a binding protein) of the present disclosure is identified or defined of the present disclosure is identified according to the Aho numbering scheme. The source of a TCR as used in the present disclosure may be from any of a variety of animal species, such as a human, mouse, rat, rabbit, or other mammal. TCR constant domain sequences may be from, for example, human, mouse, marsupial (e.g., opossum, bandicoot, wallaby), shark, or non-human primate. In certain preferred embodiments, TCR constant domain sequences are human or comprise engineered variants of human sequences. TCR constant domains may be engineered to improve pairing, expression, stability, or any combination of these. See, e.g., Cohen et al., Cancer Res, 2007; Kuball et al., Blood 2007; and Haga-Freidman et al., Journal of Immunology 2009. Examples of engineering in TCR Cα and Cβ include mutation of a native amino acid to a cysteine so that a disulfide bond forms between the introduced cysteine of one TCR constant domain and a native cysteine of the other TCR constant domain. Such mutations can include T48C in Cα, T57C in Cβ, or both. Also contemplated are embodiments wherein cognate TCR constant domains comprise mutations so that, for example, one TCR constant domain (e.g., one of Cα and Cβ) comprises an introduced "cavity" (e.g., obtainable by replacing one or more native amino acid with one or more amino acids having smaller side chains) and the other (e.g., the other of Cα and Cβ) comprises a compensatory "protuberance" (e.g., obtainable by replacing one or more native amino acid with one or more amino acids having larger side chains), similar to a "knob-into-hole" configuration used to promote preferential pairing of antibody heavy chains. Also contemplated are embodiments wherein TCR constant domain amino acids are mutated to introduce charge properties that favor pairing of the mutated constant domains. Examples of mutations that may be made in Cα and Cβ to promote specific pairing by a knobs-into-holes-type mechanism or by a charge-pairing mechanism are provided in Voss et al., J. Immunol 180(1):391-401 (2008) doi.org / 10.4049 / jimmunol.180.1.391; see also US Patent No.9,062,127. The TCR constant domain mutations, mutated TCR constant domains, and methods used to identify sites for mutation, described in these documents, are incorporated herein by reference. Mutations to improve stability can include a mutation in the Cα transmembrane domain from the sequence LSVIGF (SEQ ID NO.: 55) to the sequence LLVIVL (SEQ ID NO.: 56) ("L- V-L" mutation; see Haga-Friedman et al., J Immunol 188:5538-5546 (2012), the TCR mutations and mutant TCR constant domain sequences of which are incorporated herein by reference). As used herein, the term "CD8 co-receptor" or "CD8" means the cell surface glycoprotein CD8, either as an alpha-alpha homodimer or an alpha-beta heterodimer. The CD8 co-receptor assists in the function of cytotoxic T cells (CD8+) and functions through signaling via its cytoplasmic tyrosine phosphorylation pathway (Gao and Jakobsen, Immunol. Today 21:630-636, 2000; Cole and Gao, Cell. Mol. Immunol.1:81-88, 2004). There are five (5) human CD8 beta chain isoforms (see UniProtKB identifier P10966) and a single human CD8 alpha chain isoform (see UniProtKB identifier P01732). Non-limiting examples of human CD8 alpha and beta chain polypeptides, and polynucleotides encoding the same, are provided in herein. "CD4" is an immunoglobulin co-receptor glycoprotein that assists the TCR in communicating with antigen-presenting cells (see, Campbell & Reece, Biology 909 (Benjamin Cummings, Sixth Ed., 2002)). CD4 is found on the surface of immune cells such as T helper cells, monocytes, macrophages, and dendritic cells, and includes four immunoglobulin domains (D1 to D4) that are expressed at the cell surface. During antigen presentation, CD4 is recruited, along with the TCR complex, to bind to different regions of the MHCII molecule (CD4 binds MHCII β2, while the TCR complex binds MHCII α1 / β1). Without wishing to be bound by theory, it is believed that close proximity to the TCR complex allows CD4-associated kinase molecules to phosphorylate the immunoreceptor tyrosine activation motifs (ITAMs) present on the cytoplasmic domains of CD3. This activity is thought to amplify the signal generated by the activated TCR in order to produce or recruit various types of immune system cells, including T helper cells, and immune responses. In certain embodiments, a TCR is found on the surface of T cells (or T lymphocytes) and associates with a CD3 complex. "CD3"is a multi-protein complex of six chains (see, Abbas and Lichtman, 2003; Janeway et al., p.172 and 178, 1999) that is associated with antigen signaling in T cells. In mammals, the complex comprises a CD3γ chain, a CD3δ chain, two CD3ε chains, and a homodimer of CD3ζ chains. The CD3γ, CD3β, and CD3ε chains are related cell surface proteins of the immunoglobulin superfamily containing a single immunoglobulin domain. The transmembrane regions of the CD3γ, CD3β, and CD3ε chains are negatively charged, which is believed to allow these chains to associate with positively charged regions of T cell receptor chains. The intracellular tails of the CD3γ, CD3β, and CD3ε chains each contain a single conserved motif known as an immunoreceptor tyrosine-based activation motif or ITAM, whereas each CD3ζ chain has three. Without wishing to be bound by theory, it is believed that the ITAMs are important for the signaling capacity of a TCR complex. CD3 as used in the present disclosure may be from various animal species, including human, mouse, rat, or other mammals. As used herein, "TCR complex" refers to a complex formed by the association of CD3 with TCR. For example, a TCR complex can be composed of a CD3γ chain, a CD3β chain, two CD3ε chains, a homodimer of CD3ζ chains, a TCRα chain, and a TCRβ chain. Alternatively, a TCR complex can be composed of a CD3γ chain, a CD3β chain, two CD3ε chains, a homodimer of CD3ζ chains, a TCRγ chain, and a TCRβ chain. A "component of a TCR complex", as used herein, refers to a TCR chain (i.e., TCRα, TCRβ, TCRγ or TCRδ), a CD3 chain (i.e., CD3γ, CD3δ, CD3ε or CD3ζ), or a complex formed by two or more TCR chains or CD3 chains (e.g., a complex of TCRα and TCRβ, a complex of TCRγ and TCRδ, a complex of CD3ε and CD3δ, a complex of CD3γ and CD3ε, or a sub-TCR complex of TCRα, TCRβ, CD3γ, CD3δ, and two CD3ε chains). "Chimeric antigen receptor" (CAR) refers to a fusion protein that is engineered to contain two or more naturally occurring amino acid sequences, domains, or motifs, linked together in a way that does not occur naturally or does not occur naturally in a host cell, which fusion protein can function as a receptor when present on a surface of a cell. CARs can include an extracellular portion comprising an antigen-binding domain (e.g., obtained or derived from an immunoglobulin or immunoglobulin-like molecule, such as a TCR binding domain derived or obtained from a TCR specific for a cancer antigen, a scFv derived or obtained from an antibody, or an antigen-binding domain derived or obtained from a killer immunoreceptor from an NK cell) linked to a transmembrane domain and one or more intracellular signaling domains (optionally containing co-stimulatory domain(s)) (see, e.g., Sadelain et al., Cancer Discov., 3(4):388 (2013); see also Harris and Kranz, Trends Pharmacol. Sci., 37(3):220 (2016), Stone et al., Cancer Immunol. Immunother., 63(11):1163 (2014), and Walseng et al., Scientific Reports 7:10713 (2017), which CAR constructs and methods of making the same are incorporated by reference herein). In some embodiments, a CAR comprises a binding domain that comprises any one or more of: an antibody heavy chain variable domain (VH), an antibody light chain variable domain (VL), a VH and a VL, a single-chain variable fragment (scFv) comprising VH-linker-VL or VL-linker-VH, a fragment antigen-binding region (Fab), a single-chain Fab, an antigen- binding fragment of a heavy chain-only antibody (VHH, also referred-to as a nanobody), a killer immunoreceptor from a NK cell, a VNAR, a designed ankyrin repeat protein (DARPin (Binz et al., J. Mol. Biol.332:489, 2003 and Binz et al., Nat. Biotechnol.22:575, 2004)), a FNIII domain such as an AdnectinTM or monobody ((Richards et al., J. Mol. Biol.326:1475, 2003; Parker et al., Protein Eng. Des. Selec.18:435, 2005 and Hackel et al. (2008) J. Mol. Biol.381:1238-1252, and Chandler and Buckle, Cells 9(2):610 (2020); doi: 10.3390 / cells9030610)), a lectin binding domain, a receptor ectodomain or functional portion or fragment thereof, a ligand such as e.g. a cytokine, a fully synthetic polypeptide (e.g. designed in silico, such as using the AlphaFold modeling program), a fibrinogen domain (see, e.g., Weisel et al., Science 230:1388, 1985), a Kunitz domain (see, e.g., US Patent No.6,423,498), a cysteine-knot miniprotein (Vita et al. (1995) Proc. Nat′l. Acad. Sci. (USA) 92:6404-6408; Martin et al. (2002) Nat. Biotechnol.21:71, 2002 and Huang et al. (2005) Structure 13:755, 2005; Lui et al. Nature Communications 11:295 (2020)), a tetratricopeptide repeat domain (Main et al., Structure 11:497, 2003 and Cortajarena et al., ACS Chem. Biol.3:161, 2008), a leucine-rich repeat domain (Stumpp et al., J. Mol. Biol. 332:471, 2003), a lipocalin domain (see, e.g., WO 2006 / 095164, Beste et al., Proc. Nat′l. Acad. Sci. (USA) 96:1898, 1999 and Schönfeld et al., Proc. Nat′l. Acad. Sci. (USA) 106:8198, 2009), an armadillo repeat protein (see, e.g., Madhurantakam et al., Protein Sci.21: 1015, 2012; PCT Patent Application Publication No. WO 2009 / 040338), an affilin (Ebersbach et al., J. Mol. Biol. 372: 172, 2007), an affibody, an avimer, a knottin, a fynomer, an atrimer, cytotoxic T- lymphocyte associated protein-4 (Weidle et al., Cancer Gen. Proteo.10:155, 2013) or the like (Nord et al., Protein Eng.8:601, 1995; Nord et al., Nat. Biotechnol.15:772, 1997; Nord et al., Euro. J. Biochem.268:4269, 2001; Binz et al., Nat. Biotechnol.23:1257, 2005; Boersma and Plückthun, Curr. Opin. Biotechnol.22:849, 2011), a centyrin, or the like. A CAR typically further comprises an extracellular spacer domain (e.g., a hinge from an immunoglobulin or a CD8 co-receptor protein, or a modified version thereof, or a CH2-CH3 domain of an immunoglobulin), a transmembrane domain, and one or more intracellular signaling domain (e.g., from (e.g., human) CD3ζ, CD25, CD79A, CD79B, CARD11, DAP10, FcRα, FcRβ, FcRγ, Fyn, HVEM, ICOS, Lck, LAG3, LAT, LRP, NKG2D, NOTCH1, NOTCH2, NOTCH3, NOTCH4, Wnt, ROR2, Ryk, SLAMF1, Slp76, pTα, TCRα, TCRβ, TRIM, Zap70, PTCH2, 4 1BB, CD28, OX40, CD27, CD2, CD5, ICAM-1 (CD54), LFA-1 (CD11a / CD18), ICOS (CD278), GITR, CD30, CD40, BAFF-R, HVEM, LIGHT, MKG2C, SLAMF7, NKp80, CD160, B7-H3, a ligand that specifically binds with CD83, or any combination thereof), In some embodiments, a CAR comprises a CD3ζ signaling domain and one or both of a CD28 costimulatory domain and a 4-1BB costimulatory domain. In some cases, one or more amino acid sequence, domain, or motif of a CAR contains one or more mutation relative to a naturally occurring sequence, domain, or motif. In some embodiments, a target-binding protein comprises a “split” or “modular” CAR. "TCR / CAR" (also referred to as chimeric TCR or chTCR) refers to hybrid receptor polypeptides which comprise (1) a first polypeptide comprising a first TCR constant domain and (2) a second polypeptide comprising a second TCR constant domain, wherein the first TCR constant domain and the second TCR constant domain associate to form a dimer, and one or both of the first polypeptide and the second polypeptide comprises, amino-terminal to a constant domain, a target-binding domain that does not comprise a TCR variable domain. TCR / CARs are described in PCT / US2023 / 066466 (which published as WO2023215725), the TCR / CAR constructs of which are incorporated herein by reference. The association between the TCR constant domains can comprise one or more native interaction between cognate TCR constant domains (e.g. a native disulfide bond), one or more engineered interaction between the TCR constant domains (e.g. one or more disulfide bonds introduced by protein engineering), or both. One or both of the first polypeptide and the second polypeptide further comprises a target- binding domain N-terminal to the TCR constant domain(s). In certain embodiments of the present disclosure, one or both of the first polypeptide and the second polypeptide comprises a target-binding domain disposed N-terminal to the TCR constant domains, wherein the target binding domain is any binding domain of a CAR as described herein. In some embodiments, a target-binding domain of a TCR / CAR is selected from: (i) an antibody heavy chain variable domain (VH); (ii) an antibody light chain variable domain (VL); (iii) a single-chain variable fragment (scFv); (iv) a fragment antigen-binding region (Fab); (v) a single-chain Fab; (vi) an antigen-binding fragment of a heavy chain-only antibody (VHH) or a nanobody; (vii) a designed ankyrin repeat protein (DARPin); (viii) a fibronectin (e.g., 10FNIII) domain; (ix) a lectin binding domain; (x) a protein ligand-binding domain, such as a receptor ectodomain or a functional portion or fragment thereof; (xi) a killer immunoreceptor from a NK cell; (xii) a fibrinogen domain; (xiii) a cysteine-knot miniprotein; (xiv) a tetratricopeptide repeat domain; (xv) a leucine-rich repeat domain; (xvi) a lipocalin domain, (xvii) an armadillo repeat protein; (xviii) an affibody; (xix) an avimer; (xx) a knottin; (xxi) a fynomer; (xxii) an atrimer; (xxiii) CTLA4 (e.g., a ligand-binding domain of CTLA4); (xxiv) a synthetic protein designed to bind a natural ligand; (xxv) a ligand, such as for example a cytokine or a peptide tag; (xxvi) a centyrin; (xxvii) an affilin; or (xxviii) any combination of (i)-(xxvii). In certain embodiments, one or both of the first polypeptide and the second polypeptide comprises a target-binding domain disposed N-terminal to the TCR constant domains, wherein the target binding domain is selected from the target binding domains described herein and one or both of the first polypeptide and the second polypeptide may further comprise a TCR variable domain, provided that one or both of the first polypeptide and the second polypeptide comprise a target-binding domain that is not, or does not comprise, a TCR variable domain. TCR / CARs are preferably heterodimers (i.e., the TCR constant domains of the two polypeptides are different to one another), though TCR / CARs wherein the TCR constant domains of the two polypeptides are the same or substantially the same (e.g. are homodimeric with respect to the constant domains; see e.g. Groettrup et al. EMBO J.11(7):2735-2745 (1992)) are also contemplated. In some embodiments, the first TCR constant domain comprises a TCR alpha-chain constant domain (Cα) and the second TCR constant domain comprises a TCR beta- chain constant domain (Cβ). In other embodiments, the first TCR constant domain comprises a Cβ and the second TCR constant domain comprises a Cα. A target-binding protein can comprise a binding domain from a known target-binding protein. For example, for use in murine studies targeting FAP antigen, cross-reactive (mouse and human FAP) scFvs are known (see, e.g., Niu W, Wang B, Zhang Y, Wang C, Cao J, Li J, He Y and Lei P (2024) Efficacy and safety evaluation of cross-reactive Fibroblast activation protein scFv-based CAR-T cells. Front. Immunol.15:1433679. doi: 10.3389 / fimmu.2024.1433679), and antibodies binding murine FAP are known (see, e.g., R&D systems Catalog No. MAB9727 (Monoclonal Rat IgG1 Clone # 983802), and InVivoMab Catalog No. BE0374 (clone 73.3). "Immunomodulatory fusion protein" (IFP) refers to a fusion protein, comprising an extracellular component, a hydrophobic component, and an intracellular component, wherein the extracellular component includes a binding domain from a molecule that ordinarily, e.g., in its natural setting, is capable of delivering a negative or inhibitory signal to a host cell expressing the molecule when the molecule is bound to its binding partner or ligand or receptor, such as an immunoinhibitory receptor or checkpoint molecule, or the target is an inhibitory receptor or ligand or checkpoint molecule or other inhibitory ligand. In some embodiments, the intracellular component includes a signaling domain, such as a costimulatory signaling domain or signaling region of a molecule generally capable of delivering a costimulatory or positive signal, e.g., to an immune cell. Thus, in some aspects, an IFP is capable of delivering a positive or costimulatory signal in response to a binding event that in a natural setting would result in an inhibitory signal. Any polypeptide of this disclosure can, as encoded by a polynucleotide sequence, comprise a "signal peptide" (also known as a leader sequence, leader peptide, or transit peptide). Signal peptides target newly synthesized polypeptides to their appropriate location inside or outside the cell. In some contexts, signal peptides are from about 15 to about 22 amino acids in length. Non-limiting examples of signal peptides include: a signal peptide native to a mammalian (e.g., human) TCRα or TCRβ chain; MLLLVTSLLLCELPHPAFLLIP (SEQ ID NO.: 57) (from GM-CSF); the signal peptide MALPVTALLLPLALLLHAARP (SEQ ID NO.: 58) (from CD8α); the signal peptide MRPRLWLLLAAQLTVLHGNSV (SEQ ID NO.: 59) (from CD8β); and the signal peptide METDTLLLWVLLLWVPGSTG (SEQ ID NO.: 60) (from murine IgG kappa light chain). In some embodiments, a signal peptide from human IL-12 (e.g., MCHQQLVISWFSLVFLASPLVA (SEQ ID NO.: 61)) may be used. It will be appreciated that any suitable naturally occurring or engineered signal peptide can be employed. Certain signal peptides and characteristics of these are decribed in Owji et al., European Journal of Cell Biology 97(6):422-441 (2018), and in Ling et al. Front. Immunol. (2020) doi.org / 10.3389 / fimmu.2020.604318; the signal peptides of which are incorporated herein by reference. A signal peptide may be removed from the polypeptide during or once localization or secretion is completed. Polypeptides that have a signal peptide are referred to herein as a "pre-protein" and polypeptides having their signal peptide removed are referred to herein as "mature" proteins or polypeptides. In any of the herein disclosed embodiments, a binding protein or fusion protein comprises, or is, a mature protein, or is or comprises a pre-protein. A "linker" refers to an amino acid sequence that connects two proteins, polypeptides, peptides, domains, regions, or motifs and may provide a spacer function compatible with interaction of two sub-binding domains so that the resulting polypeptide retains a specific binding affinity (e.g., scTv, scTCR) to a target molecule or retains signaling activity (e.g., TCR complex). In certain embodiments, a linker is comprised of about two to about 35 amino acids, for instance, or about four to about 20 amino acids or about eight to about 15 amino acids or about 15 to about 25 amino acids. In certain embodiments, a linker comprises or consists of 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, or more amino acids. Exemplary linkers include glycine-serine linkers and other linkers described herein. In preferred embodiments, a linker linking two subunits of a payload molecule to one another is of sufficient length and composition that the two subunits function together substantially as they would in native payload molecule complex. In preferred embodiments, a linker linking a payload molecule (or a subunit thereof) to a CBD is of sufficient length and composition that the CBD can interact with collagen and the payload molecule or a subunit thereof is capable of performing or contributing to a desired function (e.g., function of a cytokine if the payload molecule is a cytokine). In some embodiments, a linker is or comprises a GS linker, a GSG linker, a GP linker, a GPP linker, a (GlyxSery)n linker such as comprising a GGGS sequence or a GGGGS sequence, a Townsend linker (GSGGSGGSGGTG), a linker having the sequence GSTSGSGKPGSGEGSTKG, or the like. In some embodiments, a linker consists of the sequence GGGGSGGGGSGGGGS. In some embodiments, a linker consists of the sequence GGGSGGGSGGGS. In some embodiments, a linker consists of the sequence GGSGGGSGGGSGGGS. In some embodiments, a linker consists of the sequence GGGSGGGS. In some embodiments, a linker can be about 2, 34, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 1523, 24, 25, 26, 27, 28, 29, 30, 40, 50, 60, 70, 80, 90, 100 amino acids in length, or less than about 200 amino acids in length, and can preferably be less than 25 or less than 20 amino acids in length, and will preferably comprise a flexible structure (can provide flexibility and room for conformational movement between two regions, domains, motifs, fragments, or modules connected by the linker), and will preferably be biologically inert and / or have a low risk of immunogenicity in a human. "Antigen" or "Ag" as used herein refers to an immunogenic molecule that provokes an immune response. This immune response may involve antibody production, activation of specific immunologically competent cells (e.g., T cells), or both. An antigen (immunogenic molecule) may be, for example, a peptide, glycopeptide, polypeptide, glycopolypeptide, polynucleotide, polysaccharide, lipid, or the like. It is readily apparent that an antigen can be synthesized, produced recombinantly, or derived from a biological sample. Exemplary biological samples that can contain one or more antigens include tissue samples, tumor samples, cells, biological fluids, or combinations thereof. Antigens can be produced by cells that have been modified or genetically engineered to express an antigen, or that endogenously (e.g., without modification or genetic engineering by human intervention) express a mutation or polymorphism that is immunogenic. In some embodiments, an antigen is an antigen that is expressed on the surface of a human cell (e.g., an antigen can be a human protein or a portion thereof, a human peptide, or a mutated variant thereof, or a pathogenic protein or peptide presented by an HLA). "Neoantigen," as used herein, refers to a host cellular product containing a structural change, alteration, or mutation that creates a new antigen or antigenic epitope that has not previously been observed in the subject’s genome (i.e., in a sample of healthy tissue from the subject) or been "seen" or recognized by the host's immune system, which: (a) is processed by the cell’s antigen-processing and transport mechanisms and presented on the cell surface in association with an MHC (e.g., HLA) molecule; and (b) elicits an immune response (e.g., a cellular (T cell) response). Neoantigens may originate, for example, from coding polynucleotides having alterations (substitution, addition, deletion) that result in an altered or mutated product, or from the insertion of an exogenous nucleic acid molecule or protein into a cell, or from exposure to environmental factors (e.g., chemical, radiological) resulting in a genetic change. Neoantigens may arise separately from a tumor antigen or may arise from or be associated with a tumor antigen. "Tumor neoantigen" (or "tumor specific neoantigen") refers to a protein comprising a neoantigenic determinant associated with, arising from, or arising within a tumor cell or plurality of cells within a tumor. Tumor neoantigenic determinants are found on, for example, antigenic tumor proteins or peptides that contain one or more somatic mutations or chromosomal rearrangements encoded by the DNA of tumor cells (e.g., pancreas cancer, lung cancer, colorectal cancers), as well as proteins or peptides from viral open reading frames associated with virus-associated tumors (e.g., cervical cancers, some head and neck cancers). The term "epitope" or "antigenic epitope" includes any molecule, structure, amino acid sequence or protein determinant that is recognized and specifically bound by a cognate binding molecule, such as an immunoglobulin, T cell receptor (TCR), chimeric antigen receptor, or other binding molecule, domain, or protein. Epitopic determinants generally contain chemically active surface groupings of molecules, such as amino acids or sugar side chains, and can have specific three-dimensional structural characteristics, as well as specific charge characteristics. "Major histocompatibility complex" (MHC) refers to glycoproteins that deliver peptide antigens to a cell surface of all nucleated cells. MHC class I molecules are heterodimers having a membrane spanning α chain (with three α domains) and a non-covalently associated β2 microglobulin. MHC class II molecules are composed of two transmembrane glycoproteins, α and β, both of which span the cell membrane. Each chain comprises two domains. MHC class I molecules deliver peptides originating in the cytosol to the cell surface, where a peptide:MHC complex is recognized by CD8+ T cells. MHC class II molecules deliver peptides originating in the vesicular system to the cell surface, where they are recognized by CD4+ T cells. Human MHC is referred to as human leukocyte antigen (HLA). HLAs corresponding to "class I" MHC present peptides from inside the cell and include, for example, HLA-A, HLA-B, and HLA-C. Alleles include, for example, HLA A*2, such as HLA-A*02:01. HLAs corresponding to "class II" MHC present peptides from outside the cell and include, for example, HLA-DP, HLA-DM, HLA-DOA, HLA-DOB, HLA-DQ, and HLA-DR. Principles of antigen processing by antigen presenting cells (APC) (such as dendritic cells, macrophages, lymphocytes or other cell types), and of antigen presentation by APC to T cells, including major histocompatibility complex (MHC)-restricted presentation between immunocompatible (e.g., sharing at least one allelic form of an MHC gene that is relevant for antigen presentation) APC and T cells, are well-established (see, e.g., Murphy, Janeway’s Immunobiology (8th Ed.) 2011 Garland Science, NY; chapters 6, 9 and 16). For example, processed antigen peptides originating in the cytosol (e.g., tumor antigen, intracellular pathogen) are generally from about 7 amino acids to about 11 amino acids in length and will associate with class I MHC (HLA) molecules, whereas peptides processed in the vesicular system (e.g., bacterial, viral) will vary in length from about 10 amino acids to about 25 amino acids and associate with class II MHC (HLA) molecules. Target-binding proteins of this disclosure, such as TCRs, multispecific T cell engagers, scTCRs, TRuCs (see, e.g., Bauerle et al., Nat Commun 10, 2087 (2019). https: / / doi.org / 10.1038 / s41467-019-10097-0), synNotch receptors, IFPs, and CARs, will contain a binding domain that binds a target. A "binding domain" (also referred to as a "binding region" or "binding moiety"), as used herein, refers to a molecule or portion thereof (e.g., peptide, oligopeptide, polypeptide, protein) that possesses the ability to (e.g., specifically and non- covalently) associate, unite, or combine with a target). A binding domain includes any naturally occurring, synthetic, semi-synthetic, or recombinantly produced binding partner for a biological molecule, a molecular complex (i.e., complex comprising two or more biological molecules), or other target of interest. Non-limiting examples of binding domains include immunoglobulin variable regions or single chain constructs comprising the same (e.g., single chain TCR (scTCR)). In preferred embodiments, a target-binding protein is expressed at a surface of a host cell and, optionally, delivers or initiates a signal to the host cell when bound to the target. As used herein "specifically binds" or "specific for" refers to an association or union of a target-binding protein or a binding domain to a target molecule with an affinity or Ka (i.e., an equilibrium association constant of a particular binding interaction with units of 1 / M) equal to or greater than 105 M-1 (which equals the ratio of the on-rate [kon]to the off-rate [koff] for this association reaction), while not significantly associating or uniting with any other molecules or components in a sample. Binding proteins or binding domains (or fusion proteins thereof) may be classified as "high affinity" binding proteins or binding domains (or fusion proteins thereof) or as "low affinity" binding proteins or binding domains (or fusion proteins thereof). "High affinity" binding proteins or binding domains refer to those binding proteins or binding domains having a Ka of at least 107M-1, at least 108M-1, at least 109M-1, at least 1010M-1, at least 1011M-1, at least 1012M-1, or at least 1013M-1. "Low affinity" binding proteins or binding domains refer to those binding proteins or binding domains having a Ka of up to 107M-1, up to 106M-1, or up to 105M-1. Alternatively, affinity can be defined as an equilibrium dissociation constant (Kd) of a particular binding interaction with units of M (e.g., 10-5M to 10-13M). In certain embodiments, a receptor or binding domain may have "enhanced affinity," which refers to a selected or engineered receptors or binding domain with stronger binding to a target antigen than a wild type (or parent) binding domain. For example, enhanced affinity may be due to a Ka (equilibrium association constant) for the target antigen that is higher than the wild type binding domain, due to a Kd (dissociation constant) for the target antigen that is less than that of the wild type binding domain, due to an off-rate (koff) for the target antigen that is less than that of the wild type binding domain, or a combination thereof. A variety of assays are known for identifying binding domains of the present disclosure that specifically bind a particular target, as well as determining binding domain or fusion protein affinities, such as Western blot, ELISA, analytical ultracentrifugation, spectroscopy and surface plasmon resonance (Biacore®) analysis (see, e.g., Scatchard et al., Ann. N.Y. Acad. Sci.51:660, 1949; Wilson, Science 295:2103, 2002; Wolff et al., Cancer Res.53:2560, 1993; and U.S. Patent Nos.5,283,173, 5,468,614, or the equivalent). The term "functional avidity", as used herein, refers to a biological measure or activation threshold of an in vitro immune cell (e.g., T cell, NK cell, NK-T cell) response to a given concentration of a ligand, wherein the biological measure may include or be cytokine production (e.g., IFN-γ production, IL-2 production, etc.), cytotoxic activity, activation markers (e.g., CD137, Nur77) or proliferation. For example, T cells that biologically (immunologically) respond in vitro to a low antigen dose by, for example, expressing an activation marker, producing cytokines, exhibiting cytotoxic activity, or proliferating are considered to have high or higher functional avidity, while T cells having low or lower functional avidity require higher amounts of antigen before an immune response, similar to the high-avidity T cells, is elicited. It will be understood that functional avidity is different from affinity and avidity. Affinity refers to the strength of any given bond between a binding protein and its antigen / ligand. Some binding proteins are multivalent and bind to multiple antigens – in this case, the strength of the overall connection is the avidity. Numerous correlations exist between the functional avidity and the effectiveness of an immune response. Some ex vivo studies have shown that distinct T cell functions (e.g., proliferation, cytokines production, etc.) can be triggered at different thresholds (see, e.g., Betts et al., J. Immunol.172:6407, 2004; Langenkamp et al., Eur. J. Immunol.32:2046, 2002). Factors that affect functional avidity can include (a) the affinity of a TCR for the pMHC- complex, that is, the strength of the interaction between the TCR and pMHC (Cawthon et al., J. Immunol.167:2577, 2001), (b) expression levels of the TCR, and, in some embodiments, CD4 or CD8 co receptors, on the host cell and (c) the distribution and composition of signaling molecules (Viola and Lanzavecchia, Science 273:104, 1996), as well as expression levels of molecules that attenuate T cell function and TCR signaling. The concentration of antigen needed to induce a half-maximum response (e.g., response in the form of production of a cytokine or expression of an activation marker by a host cell; or in the form of fluorescence intensity when binding to a labeled peptide:HLA multimer) between the baseline and maximum response after a specified exposure time is referred to as the "half maximal effective concentration" or "EC50". The EC50 value is generally presented as a molar (moles / liter) amount, but it is often converted into a logarithmic value as follows – log10(EC50). For example, if the EC50 equals 1 µM (10-6 M), the log10(EC50) value is –6. Another value used is pEC50, which is defined as the negative logarithm of the EC50 (-log10(EC50)). In the above example, the EC50 equaling 1 µM has a pEC50 value of 6. In certain embodiments, the functional avidity of a binding protein of this disclosure comprises a measure of an ability of the binding protein to promote activation and / or IFNγ production by host T cells, which can be measured using assays known in the art and described herein. In certain embodiments, functional avidity will comprise a measure of the ability of the binding protein, upon binding to antigen, to activate a host cell, such as a T cell. As used herein, "nucleic acid" or "nucleic acid molecule" or "polynucleotide" refers to any of deoxyribonucleic acid (DNA), ribonucleic acid (RNA), oligonucleotides, polynucleotides, fragments thereof generated, for example, by the polymerase chain reaction (PCR) or by in vitro translation, and also to fragments generated by any of ligation, scission, endonuclease action, or exonuclease action. In certain embodiments, the nucleic acids of the present disclosure are produced by PCR. Nucleic acids can be composed of monomers that are naturally occurring nucleotides (such as deoxyribonucleotides and ribonucleotides), analogs of naturally occurring nucleotides (e.g., α-enantiomeric forms of naturally occurring nucleotides), or a combination of both. Modified nucleotides can have modifications in or replacement of sugar moieties, or pyrimidine or purine base moieties. Nucleic acid monomers can be linked by phosphodiester bonds or analogs of such linkages. Analogs of phosphodiester linkages include phosphonothioate, phosphonodithioate, phosphonoselenoate, phosphorodiselenoate, phosphoroanilothioate, phosphoranilidate, phosphoramidate, and the like. Nucleic acid monomers may comprise phosphorothioate linkages, phosphorodithioate linkages, or phosphoroselenoate linkages, or any combination thereof. Nucleic acid molecules can be either single-stranded or double-stranded. In some embodiments, a polynucleotide, expression construct, or targeting polynucleotide of the present disclosure comprises or consists of DNA. In some embodiments, a polynucleotide, expression construct, or targeting polynucleotide of the present disclosure comprises or consists of RNA. In some embodiments, a polynucleotide, expression construct, or targeting polynucleotide of the present disclosure comprises or consists of mRNA. The term "isolated" means that the material is removed from its original environment (e.g., the natural environment if it is naturally occurring). For example, a naturally occurring nucleic acid or polypeptide present in a living animal is not isolated, but the same nucleic acid or polypeptide, separated from some or all of the co-existing materials in the natural system, is isolated. Such a nucleic acid could be part of a vector and / or such nucleic acid or polypeptide could be part of a composition (e.g., a cell lysate), and still be isolated in that such vector or composition is not part of the natural environment for the nucleic acid or polypeptide. Any presently disclosed T cell, host cell, fusion protein, target-binding protein, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population can be provided in an “isolated” form that is outside of a human or animal body. The term "gene" means the segment of DNA involved in producing a polypeptide chain; it includes regions preceding and following the coding region ("leader and trailer") as well as intervening sequences (introns) between individual coding segments (exons). As used herein, the terms "recombinant”, “engineered", and "modified" refer to a cell, microorganism, nucleic acid molecule, polypeptide, protein, plasmid, or vector that has been modified by introduction of an exogenous nucleic acid molecule, or refers to a cell or microorganism that has been genetically engineered by human intervention—that is, modified by introduction of a heterologous nucleic acid molecule, or refers to a cell or microorganism that has been altered such that expression of an endogenous nucleic acid molecule or gene is controlled, deregulated or constitutive, where such alterations or modifications can be introduced by genetic engineering. Human-generated genetic alterations can include, for example, modifications introducing nucleic acid molecules (which may include an expression control element, such as a promoter) encoding one or more proteins or enzymes, or other nucleic acid molecule additions, deletions, substitutions, or other functional disruption of or addition to a cell's genetic material. Exemplary modifications include those in coding regions or functional fragments thereof of heterologous or homologous polypeptides from a reference or parent molecule. As used herein, "mutation" refers to a change in the sequence of a nucleic acid molecule or polypeptide molecule as compared to a reference or wild-type nucleic acid molecule or polypeptide molecule, respectively. A mutation can result in several different types of change in sequence, including substitution, insertion or deletion of nucleotide(s) or amino acid(s). In certain embodiments, a mutation is a substitution of one or three codons or amino acids, a deletion of one to about 5 codons or amino acids, or a combination thereof. A "conservative substitution" is recognized in the art as a substitution of one amino acid for another amino acid that has similar properties. Exemplary conservative substitutions are well known in the art (see, e.g., WO 97 / 09433 at page 10; Lehninger, Biochemistry, 2ndEdition; Worth Publishers, Inc. NY, NY, pp.71-77, 1975; Lewin, Genes IV, Oxford University Press, NY and Cell Press, Cambridge, MA, p.8, 1990). In certain embodiments, a variant of a reference amino acid sequence comprises one or more conservative amino acid substitution. In certain embodiments, proteins (e.g., binding protein, immunogenic peptide) according to the present disclosure comprise a variant sequence as compared to a reference sequence (e.g., a variant cytokine as compared to a reference cytokine disclosed herein). As used herein, a "variant" amino acid sequence, peptide, or polypeptide, refers to an amino acid sequence (or peptide or polypeptide) having one or two amino acid substitutions, deletions, or insertions as compared to a reference amino acid sequence. In certain embodiments, a variant amino acid sequence, peptide, or polypeptide, retains substantially a same functionality (e.g., cytokine activity) as the reference molecule; for example, a variant cytokine as disclosed herein retains about 50%, about 60%, about 70%, about 80%, about 90%, about 95%, about 99%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, at least about 90%, at least about 95%, a least about 99%, or 100% of the activity of at least one function as compared to a reference (e.g., wild-type) cytokine. An "altered domain" or "altered protein" refers to a motif, region, domain, peptide, polypeptide, or protein with a non-identical sequence identity to a wild type motif, region, domain, peptide, polypeptide, or protein (e.g., a wild type cytokine or CBD) of at least 85% (e.g., at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9%). Altered domains or altered proteins or derivatives can include those based on all possible codon choices for the same amino acid and codon choices based on conservative amino acid substitutions. For example, the following six groups each contain amino acids that are conservative substitutions for one another: 1) alanine (ala; A), serine (ser; S), threonine (thr; T); 2) aspartic acid (asp; D), glutamic acid (glu; E); 3) asparagine (asn; N), glutamine (gln; Q); 4) arginine (arg; R), lysine (lys; K); 5) Isoleucine (ile; I), leucine (L), methionine (met; M), valine (val; V); and 6) phenylalanine (phe; F), tyrosine (tyr; Y), tryptophan (trp; W). (See also WO97 / 09433 at page 10, Lehninger, Biochemistry, 2ndEdition, Worth Publishers, Inc., NY, NY, pp.71-77, 1975; Lewin Genes IV, Oxford University Press, NY and Cell Press, Cambridge, MA, p.8, 1990; Creighton, Proteins, W.H. Freeman and Company 1984). In addition, individual substitutions, deletions, or additions that alter, add or delete, a single amino acid or a small percentage of amino acids in an encoded sequence are also "conservative substitutions." The term "construct" refers to any polynucleotide that contains a recombinant nucleic acid molecule. A "transgene" or "transgene construct" refers to a construct that contains two or more genes operably linked in an arrangement that is not found in nature. The term "operably- linked" (or "operably linked" herein) refers to the association of two or more nucleic acid molecules on a single nucleic acid fragment so that the function of one is affected by the other. For example, a promoter is operably-linked with a coding sequence when it can affect the expression of that coding sequence (i.e., the coding sequence is under the transcriptional control of the promoter). "Unlinked" means that the associated genetic elements are not closely associated with one another and the function of one does not affect the other. In some embodiments, the genes present in a transgene are operably linked to an expression control sequence (e.g., a promoter). A construct (e.g., a transgene) can be present in a vector (e.g., a bacterial vector, a viral vector) or can be integrated into a genome. A "vector" is a nucleic acid molecule that is capable of transporting another nucleic acid molecule. Vectors can be, for example, plasmids, cosmids, viruses, an RNA vector or a linear or circular DNA or RNA molecule that can include chromosomal, non-chromosomal, semi-synthetic or synthetic nucleic acid molecules. Exemplary vectors are those capable of autonomous replication (episomal vector) or expression of nucleic acid molecules to which they are linked (expression vectors). Vectors useful in the compositions and methods of this disclosure are described further herein. The term "expression", as used herein, refers to the process by which a polypeptide is produced based on the encoding sequence of a nucleic acid molecule, such as a gene. The process can include transcription, post-transcriptional control, post-transcriptional modification, translation, post-translational control, post translational modification, or any combination thereof. The term "introduced" in the context of inserting a nucleic acid molecule into a cell, means "transfection", or "transformation", or "transduction" and includes reference to the incorporation of a nucleic acid molecule into a eukaryotic or prokaryotic cell wherein the nucleic acid molecule can be incorporated into the genome of a cell (e.g., a chromosome, a plasmid, a plastid, or a mitochondrial DNA), converted into an autonomous replicon, or transiently expressed (e.g., transfected mRNA). As used herein, "heterologous" or "exogenous" nucleic acid molecule, construct or sequence refers to a nucleic acid molecule or portion of a nucleic acid molecule that is not native to a host cell but can be homologous to a nucleic acid molecule or portion of a nucleic acid molecule from the host cell. The source of the heterologous or exogenous nucleic acid molecule, construct or sequence can be from a different genus or species. In certain embodiments, a heterologous or exogenous nucleic acid molecule is added (i.e., not endogenous, or native) to a host cell or host genome by, for example, conjugation, transformation, transfection, transduction, electroporation, or the like, wherein the added molecule can integrate into the host genome or exist as extra-chromosomal genetic material (e.g., as a plasmid or other form of self-replicating vector), and can be present in multiple copies. In addition, "heterologous" refers to a non-native enzyme, protein or other activity encoded by an exogenous nucleic acid molecule introduced into the host cell, even if the host cell encodes a homologous protein or activity. Moreover, a cell comprising a "modification" or a "heterologous" polynucleotide or binding protein includes progeny of that cell, regardless of whether the progeny were themselves transduced, transfected, or otherwise manipulated or changed. As described herein, more than one heterologous or exogenous nucleic acid molecule can be introduced into a host cell as separate nucleic acid molecules, as a plurality of individually controlled genes, as a polycistronic nucleic acid molecule, as a single nucleic acid molecule encoding a fusion protein, or any combination thereof. When two or more exogenous nucleic acid molecules are introduced into a host cell, it is understood that the two or more exogenous nucleic acid molecules can be introduced as a single nucleic acid molecule (e.g., on a single vector), on separate vectors, integrated into the host chromosome at a single site or multiple sites, or any combination thereof. The number of referenced heterologous nucleic acid molecules or protein activities refers to the number of encoding nucleic acid molecules or the number of protein activities, not necessarily to the number of separate nucleic acid molecules introduced into a host cell. As used herein, the term "endogenous" or "native" refers to a gene, protein, or activity that is normally present in a host cell. Moreover, a gene, protein or activity that is mutated, overexpressed, shuffled, duplicated, or otherwise altered as compared to a parent gene, protein or activity is still considered to be endogenous or native to that particular host cell. For example, an endogenous control sequence from a first gene (e.g., a promoter, translational attenuation sequences) can be used to alter or regulate expression of a second native gene or nucleic acid molecule, wherein the expression or regulation of the second native gene or nucleic acid molecule differs from normal expression or regulation in a parent cell. The term "homologous" or "homolog" refers to a molecule or activity found in or derived from a host cell, species, or strain. For example, a heterologous or exogenous nucleic acid molecule can be homologous to a native host cell gene, and can optionally have an altered expression level, a different sequence, an altered activity, or any combination thereof. "Sequence identity," as used herein, refers to the percentage of amino acid residues or nucleobases in one sequence that are identical with the amino acid residues or nucleobases (respectively) in a reference sequence after aligning the sequences and introducing gaps, if necessary, to achieve the maximum percent sequence identity, and not considering any conservative substitutions as part of the sequence identity. The percentage sequence identity values can be generated using the NCBI BLAST 2.0 software as defined by Altschul et al. (1997), Nucl. Acids Res.25:3389-3402, with the parameters set to default values. Additionally or alternatively, the degree of sequence identity between two sequences can be determined, for example, by comparing the two sequences using computer programs designed for this purpose, such as global or local alignment algorithms. Non-limiting examples include BLASTp, BLASTn, Clustal W, MAFFT, Clustal Omega, AlignMe, Praline, GAP, BESTFIT, Needle (EMBOSS), Stretcher (EMBOSS), GGEARCH2SEQ, Water (EMBOSS), Matcher (EMBOSS), LALIGN, SSEARCH2SEQ, or another suitable method or algorithm. A global alignment algorithm, such as a Needleman and Wunsch algorithm, can be used to align two sequences over their entire length, maximizing the number of matches and minimizes the number of gaps. Default settings can be used. To generate similarity scores for two amino acid sequences, scoring matrices can be used that assign positive scores for some non-identical amino acids (e.g., conservative amino acid substitutions, amino acids with similar physio-chemical properties, and / or amino acids that exhibit frequent substitutions in orthologs, homologs, or paralogs), Non-limiting examples of scoring matrices include PAM30, PAM70, PAM250, BLOSUM45, BLOSUM50, BLOUM62, BLOSUM80, and BLOSUM90. Variants of nucleic acid molecules of this disclosure are also contemplated. Variant nucleic acid molecules are at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, and are preferably at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or at least 99.9% identical a nucleic acid molecule of a defined or reference polynucleotide as described herein, or that hybridize to a polynucleotide under stringent hybridization conditions of 0.015 M sodium chloride, 0.0015 M sodium citrate at about 65-68ºC or 0.015 M sodium chloride, 0.0015 M sodium citrate, and 50% formamide at about 42ºC. Nucleic acid molecule variants retain the capacity to encode a binding protein or a binding domain thereof having a functionality described herein, such as binding a target molecule. In some contexts, the term "variant" as used herein, refers to at least one fragment of the full-length sequence referred to, more specifically one or more amino acid or nucleic acid sequence which is, relative to the full-length sequence, truncated at one or both termini by one or more amino acids. Such a fragment includes or encodes for a peptide having at least 6, least 7, least 8, least 10, least 12, least 15, least 20, least 25, least 50, least 75, least 100, least 150, or least 200 successive amino acids of the original sequence or a variant thereof. The total length of the variant may be at least 6, least 7, least 8, least 9, least 10, least 11, least 12, least 20, least 25, least 30, least 40, least 50, least 60, least 70, least 80, least 90, least 100, or more amino acids. In some embodiments, a variant polypeptide or polynucleotide has at least %, at least 92%, at least 93%, at least at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or at least 99.5% identity to a reference polypeptide or polynucleotide of the same length. In some embodiments, the term "variant" relates not only to at least one fragment, but also to a polypeptide or a fragment thereof including amino acid sequences that are at least 40%, at least 50%, at least 60%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or at least 99.5% identical to the reference amino acid sequence referred to or the fragment thereof, wherein amino acids other than those essential for the biological activity or the fold or structure of the polypeptide are deleted or substituted, one or more such essential amino acids are replaced in a conservative manner, and / or amino acids are added such that the biological activity of the polypeptide is preserved. The state of the art includes various methods that may be used to align two given nucleic acid or amino acid sequences and to calculate the degree of identity (see, e.g., Arthur Lesk (2008), Introduction to Bioinformatics, Oxford University Press, 2008, 3rd edition). In some embodiments, the Clustal W software can be used using default settings (Larkin, M. A., et al. (2007). Clustal W and Clustal X version 2.0. Bioinformatics, 23, 2947–2948). Other methods and programs for these purposes are known in the art and described herein. In certain embodiments, variants may, in addition, include chemical modifications, for example, isotopic labels or covalent modifications such as glycosylation, phosphorylation, acetylation, decarboxylation, citrullination, hydroxylation and the like. Methods for modifying polypeptides are known and in general will be employed so as not to abolish or substantially diminish a desired activity of the polypeptide. In an embodiment, the term "variant" of a nucleic acid molecule includes nucleic acids the complementary strand of which hybridizes, for example, under stringent conditions, to the reference or wild type nucleic acid. Stringency of hybridization reactions is readily determinable by one of ordinary skill in the art, and in general is an empirical calculation dependent on probe length, washing temperature, and salt concentration. In general, longer probes require higher temperatures for proper annealing, while shorter probes less so. Hybridization generally depends on the ability of denatured DNA to reanneal to complementary strands present in an environment below their melting temperature: the higher the degree of desired homology between the probe and hybridizable sequence, the higher the relative temperature which may be used. As a result, higher relative temperatures would tend to make the reaction conditions more stringent, while lower temperature less so. For additional details and explanation of stringency of hybridization reactions, see Ausubel, F. M. (1995), Current Protocols in Molecular Biology. John Wiley & Sons, Inc. Moreover, the person skilled in the art may follow the instructions given in the manual Boehringer Mannheim GmbH (1993) The DIG System Users Guide for Filter Hybridization, Boehringer Mannheim GmbH, Mannheim, Germany and in Liebl, W., Ehrmann, M., Ludwig, W., and Schleifer, K. H. (1991) International Journal of Systematic Bacteriology 41: 255-260 on how to identify DNA sequences by means of hybridization. In an embodiment, stringent conditions are applied for any hybridization, i.e., hybridization occurs only if the probe is 70% or more identical to the target sequence. Probes having a lower degree of identity with respect to the target sequence may hybridize, but such hybrids are unstable and will be removed in a washing step under stringent conditions, for example, lowering the concentration of salt to 2× SSC or, optionally and subsequently, to 0.5× SSC, while the temperature is, for example, about 50 °C–68 °C, about 52 °C–68 °C, about 54 °C–68 °C, about 56 °C–68 °C, about 58 °C–68 °C, about 60 °C–68 °C, about 62 °C–68 °C, about 64 °C–68 °C, or about 66 °C–68 °C. In an embodiment, the temperature is about 64 °C–68 °C or about 66 °C–68 °C. It is possible to adjust the concentration of salt to 0.2× SSC or even 0.1× SSC. Nucleic acid sequences having a degree of identity with respect to the reference or wild type sequence of at least 70%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or at least 99.5% may be isolated. In an embodiment, the term variant of a nucleic acid sequence, as used herein, refers to any nucleic acid sequence that encodes the same amino acid sequence and variants thereof as the reference nucleic acid sequence, in line with the degeneracy of the genetic code. A "functional variant" refers to a polypeptide or polynucleotide that is structurally similar or substantially structurally similar to a parent or reference compound of this disclosure, but differs, in some contexts slightly, in composition (e.g., one base, atom or functional group is different, added, or removed; or one or more amino acids are mutated, inserted, or deleted), such that the polypeptide or encoded polypeptide is capable of performing at least one function of the encoded parent polypeptide with at least 50% efficiency, preferably at least 55%, at least 60%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 99.9%, or at least 100% level of activity of the parent polypeptide. In other words, a functional variant of a polypeptide or encoded polypeptide of this disclosure has "similar binding," "similar affinity" or "similar activity" when the functional variant displays no more than a 50% reduction in performance in a selected assay as compared to the parent or reference polypeptide, such as an assay for measuring binding affinity (e.g., Biacore® or tetramer staining measuring an association (Ka) or a dissociation (KD) constant), avidity, or activation of a host cell. As used herein, a "functional portion" or "functional fragment" refers to a polypeptide or polynucleotide that comprises only a domain, motif, portion or fragment of a parent or reference compound, and the polypeptide or encoded polypeptide retains at least 50% activity associated with the domain, portion or fragment of the parent or reference compound, preferably at least 55%, at least 60%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99 at least %, 99.9%, or at least 100% level of activity of the parent polypeptide, or provides a biological benefit (e.g., effector function). A "functional portion" or "functional fragment" of a polypeptide or encoded polypeptide of this disclosure has "similar binding" or "similar activity" when the functional portion or fragment displays no more than a 50% reduction in performance in a selected assay as compared to the parent or reference polypeptide (preferably no more than 20% or 10%, or no more than a log difference as compared to the parent or reference with regard to affinity), such as an assay for measuring binding affinity or measuring effector function (e.g., cytokine release). Functional variants of specifically disclosed binding proteins and polynucleotides are contemplated. An “altered domain” or “altered protein” refers to a motif, region, domain, peptide, polypeptide, or protein with a non-identical sequence identity to a wild type motif, region, domain, peptide, polypeptide, or protein (e.g., a wild type TCRα chain, TCRβ chain, TCRα constant domain, or TCRβ constant domain) of at least 85% (e.g., at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, at least 99.1%, at least 99.2%, at least 99.3%, at least 99.4%, at least 99.5%, at least 99.6%, at least 99.7%, at least 99.8%, or at least 99.9%). The present disclosure includes the following, non-limiting, Enumerated Embodiments. Any of these Embodiments may be combined with any other Embodiment or Embodiments, in any combination. The Embodiments and combinations thereof can be combined with other aspects and embodiments of the present disclosure. Embodiment 1. A T cell encoding or expressing: (i) a fusion protein that comprises, consists essentially of, or consists of a collagen- binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the T cell encodes or expresses the cytokine; and (ii) a target-binding protein, wherein the target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR) that is optionally heterologous to the T cell, a single-chain TCR (scTCR), a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP). Embodiment 2. A host cell encoding or expressing a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the host cell encodes or expresses the cytokine, and wherein the host cell comprises a T cell. Embodiment 3. The T cell of Embodiment 1 or the host cell of Embodiment 2, wherein the T cell comprises a human T cell. Embodiment 4. The T cell of Embodiment 1 or 3 or the host cell of Embodiment 2 or 3, wherein the T cell comprises a CD4+ T cell, a CD8+ T cell, a CD4- CD8- double negative T cell, a γδ T cell, a naïve T cell, a central memory T cell, a stem cell memory T cell, an effector memory T cell, or any combination thereof. Embodiment 5. The T cell of Embodiment 4 or the host cell of Embodiment 4, wherein the T cell comprises a CD8+ T cell, a CD4+ T cell, or both. Embodiment 6. A host cell encoding or expressing a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the host cell encodes or expresses the cytokine, and wherein the host cell comprises a human cell. Embodiment 7. A host cell encoding or expressing a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the host cell encodes or expresses the cytokine, and wherein the host cell comprises a hematopoietic progenitor cell, a stem cell, a peripheral blood mononuclear cell (PBMC), a tumor infiltrating lymphocyte (TIL), or any combination thereof. Embodiment 8. A host cell encoding or expressing a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the host cell encodes or expresses the cytokine, wherein the host cell comprises an immune system cell, optionally comprising a T cell, a NK cell, a NK-T cell, a dendritic cell, a macrophage, a B cell, a monocyte, or any combination thereof. Embodiment 9. The host cell of Embodiment 7 or 8, wherein the host cell is a human cell. Embodiment 10. The host cell of any one of Embodiments 2-9, wherein the host cell further encodes or expresses a target-binding protein, wherein the target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR) that is optionally heterologous to the host cell, a single-chain TCR, a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP). Embodiment 11. The T cell of Embodiment 1, 3, 4, or 5, or the host cell of Embodiment 10, wherein the target-binding protein is encoded by a polynucleotide or expression construct that also encodes the fusion protein and wherein, optionally, (1) a nucleotide sequence encoding the fusion protein is operably linked to a promoter, wherein, further optionally, (1) the promoter comprises a NFAT binding site and / or is an inducible promoter responsive to NFAT binding to a NFAT binding site and the polynucleotide or expression construct comprises one, two, three, four, five, six, or more NFAT binding sites, one or more of which is operably linked to the inducible promoter, and / or (2) a nucleotide sequence encoding the target-binding protein is operably linked to a constitutive promoter. Embodiment 12. A polynucleotide encoding (i) a payload (e.g., a cytokine), wherein at least a portion (e.g., a subunit) of the payload (e.g., cytokine) is linked to or is directly fused to a collagen-binding domain (CBD), forming a fusion protein, and (ii) a target-binding protein, wherein the target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR), a single-chain TCR, a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP), wherein, optionally: (1) the polynucleotide is codon-optimized for expression in a human T cell; and / or (2) the polynucleotide comprises a promoter operably linked to a nucleotide sequence encoding the target-binding protein, wherein, further optionally, the promoter comprises a constitutive promoter; and / or (3) the polynucleotide comprises a promoter operably linked to a nucleotide sequence encoding the payload (e.g., cytokine) or a portion thereof, wherein, optionally, the promoter comprises a NFAT binding site and / or is an inducible promoter responsive to NFAT binding to a NFAT binding site and the polynucleotide comprises one, two, three, four, five, six, or more NFAT binding sites, one or more of which is operably linked to the inducible promoter; and / or (4) the payload (e.g., cytokine) comprises a plurality of subunits, the polynucleotide encodes each of the plurality of subunits, and one or more of the plurality of subunits is linked or is directly fused to one or more CBD, further optionally wherein, between nucleotide sequences encoding the plurality of subunits, are nucleotide sequences that each independently encode a cleavage sequence (e.g., 2A self-cleaving peptide sequence, furin cleavage site) and / or comprise an IRES. Embodiment 13. An expression construct comprising a promoter operably linked to a nucleotide sequence encoding a fusion protein that comprises, consists essentially of, or consists of: a collagen-binding domain (CBD) linked or directly fused to a payload (e.g., a cytokine or a portion thereof (e.g., to a subunit of the cytokine)), wherein the promoter comprises a NFAT binding site and / or is an inducible promoter operably linked to one or more NFAT binding sites of the expression construct, wherein, optionally, (1) a NFAT-binding site comprises, consists essentially of, or consists of the nucleotide sequence Ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 20), and / or the expression construct comprises two, three, four, five, six, or more NFAT-binding sites, wherein, further optionally, each of the two, three, four, five, six, or more NFAT-binding sites comprises, consists essentially of, or consists of the nucleotide sequence Ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 20), wherein, even further optionally, the expression construct comprises the following nucleotide sequence: Ggaggaaaaactgtttcatacagaaggcgtggaggaaaaactgtttcatacagaaggcgtggaggaaaaactgtttcatacagaaggcgt ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 21), and / or (2) the promoter comprises, consists essentially of, or consists of the nucleotide sequence tagagggtatataatggaagctcgatttccag (SEQ ID NO.: 22); and / or (3) the payload (e.g., cytokine) comprises a plurality of subunits, the expression vector encodes each of the plurality of subunits, and one or more of the plurality of subunits is linked or is directly fused to one or more CBD, further optionally wherein, between nucleotide sequences encoding the plurality of subunits, are nucleotide sequences that each independently encode a cleavage sequence (e.g., 2A self-cleaving peptide sequence, furin cleavage site, or the like) and / or comprise an IRES; and / or (4) the expression construct further encodes a target-binding protein, wherein the target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR), a single-chain TCR, a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP), wherein a nucleotide sequence encoding the target-binding protein is operably linked to a promoter, wherein, further optionally, the promoter is a constitutive promoter and / or is a SFFV, PGK, EF1-alpha, CAG, MNDU3, CMV, CMV + intron, EFS, CBA, MSCV, MNDU3, SV40, mPGK, hPGK, UBC or CBh promoter. Embodiment 14. The T cell of Embodiment 1, 3, 4, 5, or 11, the host cell of any one of Embodiments 2-11, or the polynucleotide of Embodiment 12, wherein a promoter comprises a NFAT binding site and / or is operably linked to one or more NFAT binding site, the promoter being operably linked to a polynucleotide encoding the fusion protein, wherein, optionally, (1) an NFAT-binding site comprises, consists essentially of, or consists of the nucleotide sequence Ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 20), and / or the expression construct comprises two, three, four, five, six, or more NFAT-binding sites, wherein, further optionally, each of the two, three, four, five, six, or more NFAT-binding sites comprises, consists essentially of, or consists of the nucleotide sequence Ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 20), wherein, even further optionally, the expression construct comprises the following nucleotide sequence: Ggaggaaaaactgtttcatacagaaggcgtggaggaaaaactgtttcatacagaaggcgtggaggaaaaactgtttcatacagaaggcgt ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 21), and / or (2) the promoter comprises, consists essentially of, or consists of the nucleotide sequence tagagggtatataatggaagctcgatttccag (SEQ ID NO.: 22), and / or (3) a nucleotide sequence encoding the target-binding protein is operably linked to a promoter, wherein, further optionally, the promoter is a constitutive promoter and / or is a SFFV, PGK, EF1-alpha, CAG, MNDU3, CMV, CMV + intron, EFS, CBA, MSCV, MNDU3, SV40, mPGK, hPGK, UBC or CBh promoter. Embodiment 15. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14, the host cell of any one of Embodiments 2-11 and 14, the polynucleotide of Embodiment 12 or 14, or the expression construct of Embodiment 13, wherein the fusion protein comprises a single CBD. Embodiment 16. The T cell of Embodiment 15, the host cell of Embodiment 15, the polynucleotide of Embodiment 15, or the expression construct of Embodiment 15, wherein the single CBD is linked to or is directly fused to an amino-terminal end of the cytokine or a portion thereof. Embodiment 17. The T cell of Embodiment 15, the host cell of Embodiment 15, the polynucleotide of Embodiment 15, or the expression construct of Embodiment 15, wherein the single CBD is linked to or is directly fused to a carboxy-terminal end of the cytokine or a portion thereof. Embodiment 18. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14, the host cell of any one of Embodiments 2-11 and 14, the polynucleotide of Embodiment 12 or 14, or the expression construct of Embodiment 13, wherein the fusion protein comprises two CBDs, wherein the two CBDs are the same or are different, and wherein the fusion protein optionally comprises only two CBDs, further optionally wherein the only two CBDs are the same. Embodiment 19. The T cell of Embodiment 18, the host cell of Embodiment 18, the polynucleotide of Embodiment 18, or the expression construct of Embodiment 18, wherein the fusion protein comprises one CDB linked to or directly fused to an amino-terminal end of the cytokine or a portion thereof and one CBD linked to or directly fused to a carboxy-terminal end of the cytokine or a portion thereof. Embodiment 20. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14-19, the host cell of any one of Embodiments 2-11 and 14-19, the polynucleotide of any one of Embodiments 12 and 14-19, or the expression construct of any one of Embodiments 13 and 15- 19, wherein the fusion protein comprises a CBD linked to the cytokine or a portion thereof by a linker, wherein, optionally, the linker has a length of from about 4 to about 16 amino acids and / or wherein the linker comprises a GlyxSery amino acid sequence, wherein, further optionally, the linker comprises, consists essentially of, or consists of the amino acid sequence GGGSGGGS (SEQ ID NO.: 7). Embodiment 21. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14-20, the host cell of any one of Embodiments 2-11 and 14-20, the polynucleotide of any one of Embodiments 12 and 14-20, or the expression construct of any one of Embodiments 13 and 15- 20, wherein the fusion protein comprises a CBD directly fused to the cytokine or a portion thereof, wherein, optionally, a CBD is directly fused to an amino-terminal end of the cytokine or a portion thereof, and / or a CBD is directly fused to a carboxy-terminal end of the cytokine or a portion thereof. Embodiment 22. The T cell of Embodiment 18 or 19, the host cell of Embodiment 18 or 19, the polynucleotide of Embodiment 18 or 19, or the expression construct of Embodiment 18 or 19, wherein the fusion protein comprises two CBDs, wherein one CBD is linked to an amino-terminal end of the cytokine or a portion thereof by a first linker and one CBD is linked to a carboxy-terminal end of the cytokine or a portion thereof by a second linker, wherein the first linker and the second linker are the same or are different. Embodiment 23. The T cell of Embodiment 18 or 19, the host cell of Embodiment 18 or 19, the polynucleotide of Embodiment 18 or 19, or the expression construct of Embodiment 18 or 19, wherein the fusion protein comprises two CBDs, wherein one CBD is linked to the cytokine or a portion thereof by a linker and one CBD is directly fused to the cytokine or a portion thereof. Embodiment 24. The T cell of Embodiment 18 or 19, the host cell of Embodiment 18 or 19, the polynucleotide of Embodiment 18 or 19, or the expression construct of Embodiment 18 or 19, wherein the fusion protein comprises two CBDs, wherein each of the two CBDs is directly fused to the cytokine or a portion thereof , optionally one CBD being directly fused to an amino-terminal end of the cytokine or a portion thereof and one CBD being directly fused to a carboxy-terminal end of the cytokine or a portion thereof. Embodiment 25. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14-24, the host cell of any one of Embodiments 2-11 and 14-24, the polynucleotide of any one of Embodiments 12 and 14-24, or the expression construct of any one of Embodiments 13 and 15- 24, wherein the cytokine is an proinflammatory cytokine. Embodiment 26. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14-24, the host cell of any one of Embodiments 2-11 and 14-24, the polynucleotide of any one of Embodiments 12 and 14-24, or the expression construct of any one of Embodiments 13 and 15- 24, wherein the cytokine comprises any one or more of, or is selected from: IL-12, IL-1, IL-2, IL-3, IL-4, IL-5, IL-6, IL-7, IL-8, IL-9, IL-10, IL-11, IL-13, IL-14, IL-15, IL-16, IL-17, IL-18, IL-19, IL-20, IL-21, IL-22, IL-23, IL-24, IL-25, IL-26, IL-27, IL-28, IL-29, IL-30, IL-31, IL-32, IL-33, IL-34, IL-35, IL-36, IL-37, IL-38, IL-39, TNF-α, TNF-β, IFNα, IFNβ, IFNγ, CCL1, CCL2, CCL3, CCL4, CCL5, CCL7, CCL8, CCL9, CCL10, CCL11, CCL12, CCL13, CCL14, CCL15, CCL16, CCL17, CCL18, CCL19, CCL20, CCL21, CXCL1, CXCL2 ,CXCL3, CXCL4, CXCL5, CXCL6, CXCL7, CXCL8, CXCL9, CXCL10, CXCL11, CXCL12, CXCL13, CXCL14, CXCL15, CXCL16, CXCL17, GM-CSF, G-CSF, TRAIL, FASL, and a functional portion or variant of any of the foregoing. Embodiment 27. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14-26, the host cell of any one of Embodiments 2-11 and 14-26, the polynucleotide of any one of Embodiments 12 and 14-26, or the expression construct of any one of Embodiments 13 and 15- 26, wherein the cytokine is a human cytokine or is derived from a human cytokine. Embodiment 28. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14-27, the host cell of any one of Embodiments 2-11 and 14-27, the polynucleotide of any one of Embodiments 12 and 14-27, or the expression construct of any one of Embodiments 13 and 15- 27, wherein the cytokine comprises a plurality of subunits and two or more of the plurality of subunits are linked to or are directly fused to one another in a fusion protein. Embodiment 29. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14-28, the host cell of any one of Embodiments 2-11 and 14-28, the polynucleotide of any one of Embodiments 12 and 14-28, or the expression construct of any one of Embodiments 13 and 15- 28, wherein the cytokine comprises an (e.g., human) IL-12, a TNFα, an IL-7, a CCL4, and / or an IFNγ. Embodiment 30. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14-29, the host cell of any one of Embodiments 2-11 and 14-29, the polynucleotide of any one of Embodiments 12 and 14-29, or the expression construct of any one of Embodiments 13 and 15- 29, wherein the cytokine comprises a plurality of subunits, wherein a first subunit and a second subunit are linked by a linker or are directly fused to one another. Embodiment 31. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14-30, the host cell of any one of Embodiments 2-11 and 14-30, the polynucleotide of any one of Embodiments 12 and 14-30, or the expression construct of any one of Embodiments 13 and 15- 30, wherein the cytokine comprises a plurality of subunits, wherein each of the plurality of subunits is linked or is to directly fused to another of the plurality of subunits. Embodiment 32. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14-31, the host cell of any one of Embodiments 2-11 and 14-31, the polynucleotide of any one of Embodiments 12 and 14-31, or the expression construct of any one of Embodiments 13 and 15- 31, wherein the cytokine comprises an IL-12, preferably a human IL-12. Embodiment 33. The T cell of Embodiment 32, the host cell of Embodiment 32, the polynucleotide of Embodiment 32, or the expression construct of Embodiment 32, wherein a p40 subunit of the IL-12 is fused or linked directly to a CBD and / or wherein a p35 subunit of the IL- 12 is fused or directly linked to a CBD. Embodiment 34. The T cell of Embodiment 32 or 33, the host cell of Embodiment 32 or 33, the polynucleotide of Embodiment 32 or 33, or the expression construct of Embodiment 32 or 33, wherein a p40 subunit of the IL-12 is linked to a p35 subunit of the IL-12 to form a fusion protein (single-chain IL-12 or scIL-12), optionally wherein a linker links a C- terminal end of the p40 subunit to a N-terminal end of the p35 subunit. Embodiment 35. The T cell of any one of Embodiments 32-34, the host cell of any one of Embodiments 32-34, the polynucleotide of any one of Embodiments 32-34, or the expression construct of any one of Embodiments 32-34, wherein a nucleotide sequence encoding a p40 subunit of the IL-12 is disposed 5’ of a nucleotide sequence encoding a p35 subunit of the IL-12. Embodiment 36. The T cell of any one of Embodiments 32-34, the host cell of any one of Embodiments 32-34, the polynucleotide of any one of Embodiments 32-34, or the expression construct of any one of Embodiments 32-34, wherein a nucleotide sequence encoding a p40 subunit of the IL-12 is disposed 3’ of a nucleotide sequence encoding a p35 subunit of the IL-12. Embodiment 37. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14-36, the host cell of any one of Embodiments 2-11 and 14-36, the polynucleotide of any one of Embodiments 12 and 14-36, or the expression construct of any one of Embodiments 13 and 15- 36, wherein the cytokine and / or the fusion protein comprises a linker, wherein the linker optionally comprises, consists essentially of, or consists of any one or more of: a glycine-serine linker (e.g., (GlyxSery)n, wherein x, y, and n are each independently an integer selected from 1 to 10); a proline-glycine linker; an elastin or elastin-like linker (e.g., comprising or consisting of the sequence (VPGXG)n (SEQ ID NO.: 62), wherein X is any amino acid other than proline, and n represents the number of pentapeptide repeats, such as for example an integer selected from 1, 2, 3, 4, 5, and 6, or an integer from 1 to 5, or an integer from 1 to 6); a Whitlow linker (GSTSGSGKPGSGEGSTKG (SEQ ID NO.: 63)); a Townsend linker (GSGGSGGSGGTG (SEQ ID NO.: 64)); a linker comprising, consisting essentially of, or consisting of the sequence GSGKPGSGEG (SEQ ID NO.: 65); a linker comprising, consisting essentially of, or consisting of the sequence GKPGSGEG (SEQ ID NO.: 66); SGKPGSGE (SEQ ID NO.: 67); a linker comprising, consisting essentially of, or consisting of a sequence BPXXXZ (SEQ ID NO.: 68), wherein each X is independently a glycine (G) or serine (S), B is a positively charged amino acid and Z is glycine (G) or a negatively charged amino acid; a linker comprising, consisting essentially of, or consisting of the sequence GSTSGGGSGGGSGGGGSS (SEQ ID NO.: 69); a linker comprising, consisting essentially of, or consisting of the sequence EGKSSGSGSESKVD (SEQ ID NO.: 70). Embodiment 38. The T cell of any one of Embodiments 32-37, the host cell of any one of Embodiments 32-37, the polynucleotide of any one of Embodiments 32-37, or the expression construct of any one of Embodiments 32-37, wherein the IL-12 comprises a single chain fusion protein (scIL-12) wherein a p40 subunit of an optionally human IL-12, or a functional fragment or variant thereof, is linked by a linker to a p35 subunit of an optionally human IL-12, or a functional variant or fragment thereof, wherein: the scIL-12 comprises, in amino-terminal to carboxy-terminal direction: the p40 subunit, or a functional fragment or variant thereof; the linker; and the p35 subunit, or a functional fragment or variant thereof; and / or the linker comprises a (GlyxSery)n sequence, wherein x, y, and n are each independently an integer selected from 1 to 10, and / or has a length of from about 10 to about 25 amino acids, preferably about 15 amino acids, wherein, further optionally, the linker comprises, consists essentially of, or consists of the sequence GGGGSGGGGSGGGGS (SEQ ID NO.: 8); and / or the linker comprises any one or more of: a proline-glycine linker; an elastin or elastin-like linker (e.g., comprising or consisting of the sequence (VPGXG)n (SEQ ID NO.: 62), wherein X is any amino acid other than proline, and n represents the number of pentapeptide repeats, such as for example an integer selected from 1, 2, 3, 4, 5, and 6, or an integer from 1 to 5, or an integer from 1 to 6); a Whitlow linker (GSTSGSGKPGSGEGSTKG (SEQ ID NO.: 63)); a Townsend linker (GSGGSGGSGGTG (SEQ ID NO.: 64)); a linker comprising, consisting essentially of, or consisting of the sequence GSGKPGSGEG (SEQ ID NO.: 65); a linker comprising, consisting essentially of, or consisting of the sequence GKPGSGEG (SEQ ID NO.: 66); SGKPGSGE (SEQ ID NO.: 67); a linker comprising, consisting essentially of, or consisting of a sequence BPXXXZ (SEQ ID NO.: 68), wherein each X is independently a glycine (G) or serine (S), B is a positively charged amino acid and Z is glycine (G) or a negatively charged amino acid; a linker comprising, consisting essentially of, or consisting of the sequence GSTSGGGSGGGSGGGGSS (SEQ ID NO.: 69); a linker comprising, consisting essentially of, or consisting of the sequence EGKSSGSGSESKVD (SEQ ID NO.: 70). Embodiment 39. A host cell encoding or expressing a fusion protein comprising (i) a collagen-binding domain (CBD) and (ii) a payload portion, wherein the host cell comprises a human cell, a human immune cell, a tumor infiltrating lymphocyte (TIL), a hematopoietic progenitor cell, a stem cell, a peripheral blood mononuclear cell (PBMC), a T cell, a NK cell, a NK-T cell, a macrophage, a monocyte, a dendritic cell, a B cell, or any combination thereof, and wherein, optionally, the payload portion comprises an antibody or an antigen-binding fragment thereof, a cytokine, a toxin, a polypeptide that inhibits an interaction between two or more proteins, a detectable agent such as a tag or a fluorescent marker, or any combination thereof. Embodiment 40. The host cell of Embodiment 39, wherein the T cell comprises a CD4+ T cell, a CD8+ T cell, a CD4- CD8- double negative T cell, a γδ T cell, a naïve T cell, a central memory T cell, a stem cell memory T cell, an effector memory T cell, or any combination thereof. Embodiment 41. The host cell of Embodiment 40, wherein the T cell comprises a CD8+ T cell, a CD4+ T cell, or both. Embodiment 42. The T cell of any one of Embodiments 1, 3, 4, 5, 11, and 14-38, the host cell of any one of Embodiments 2-11 and 14-41, the polynucleotide of any one of Embodiments 12 and 14-38, or the expression construct of any one of Embodiments 13 and 15- 38, wherein the / a CBD comprises a CBD from or derived from: a von Willebrand Factor (vWF) A3 domain; a vWF A1 domain; a decorin; a lumican; a fibronectin; a placental growth factor (PlGF), such as PlGF1 or PlGF2; a collagen-binding peptide (e.g., comprising, consisting essentially of, or consisting of the amino acid sequence TKKTLRT (SEQ ID NO.: 48), and / or comprising, consisting essentially of, or consisting of the amino acid sequence LRELHLNNN (SEQ ID NO.: 49) and / or comprising, consisting essentially of, or consisting of the amino acid sequence WREPFSMALS (SEQ ID NO.: 50)), a bacterial surface protein (e.g., lipoprotein SLR, M protein, or M-like protein); a collagen mimetic peptide (CMP); an avimer; an antibody or antigen-binding fragment thereof; or a combination of any two or more of the foregoing. Embodiment 43. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38 and 42, the host cell of any one of Embodiments 2-11 and 14-42, the polynucleotide of any one of Embodiments 12, 14-38 and 42, or the expression construct of any one of Embodiments 13 and 15-38 and 42, wherein: (i) the fusion protein comprises a CBD that has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity or homology or similarity to, and / or comprises one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, or twenty amino acid substitutions, insertions, and / or deletions as compared to, to the amino acid sequence CSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDV PWNVVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTD VSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMV TLGNSFLHKLCSGFVRI (SEQ ID NO.: 5); and / or (ii) the CBD comprises, consists essentially of, or consists of the amino acid sequence CSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNV VPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTDVSVD SVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMVTLGN SFLHKLCSGFVRI (SEQ ID NO.: 5); (iii) the fusion protein comprises a p40 subunit of a human IL-12, or a functional portion or variant thereof that has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity or homology or similarity to, and / or comprises one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, or twenty amino acid substitutions, insertions, and / or deletions as compared to, to the amino acid sequence IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLT IQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKN YSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQE DSACPAAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSW EYPDTWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYS SSWSEWASVPCS (SEQ ID NO.: 3); and / or (iv) the fusion protein comprises a p35 subunit of a human IL-12, or a functional portion or variant thereof that has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity or homology or similarity to, and / or comprises one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, or twenty amino acid substitutions, insertions, and / or deletions as compared to, to the amino acid sequence RNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKD KTSTVEACLPLELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEF KTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCIL LHAFRIRAVTIDRVMSYLNAS (SEQ ID NO.: 4); and / or (v) fusion protein comprises an amino acid sequence that has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity or homology or similarity to, and / or comprises one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, or twenty amino acid substitutions, insertions, and / or deletions as compared to, to the amino acid sequence IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLT IQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKN YSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQE DSACPAAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSW EYPDTWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYS SSWSEWASVPCSXRNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEI DHEDITKDKTSTVEACLPLELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYED LKMYQVEFKTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDF YKTKIKLCILLHAFRIRAVTIDRVMSYLNAS (SEQ ID NO.: 71), wherein X is present or absent and, if present, is a linker that optionally comprises a (GlyxSery)n sequence and / or has a length of from about 10 to about 25 amino acids, preferably about 15 amino acids, wherein, further optionally, the linker comprises, consists essentially of, or consists of the sequence GGGGSGGGGSGGGGS (SEQ ID NO.: 8); and / or (vi) the fusion protein comprises the amino acid sequence IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKE FGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRF TCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACP AAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPD TWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWS EWASVPCSXRNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHED ITKDKTSTVEACLPLELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMY QVEFKTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKI KLCILLHAFRIRAVTIDRVMSYLNAS (SEQ ID NO.: 71), wherein X is present or absent and, if present, is a linker that optionally comprises a GlyxSery sequence and / or has a length of from about 10 to about 25 amino acids, preferably about 15 amino acids, wherein, further optionally, the linker comprises, consists essentially of, or consists of the sequence GGGGSGGGGSGGGGS (SEQ ID NO.: 8); and / or (vii) the fusion protein comprises, consists essentially of, or consists of an amino acid sequence that has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity or homology or similarity to, and / or comprises one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, or twenty amino acid substitutions, insertions, and / or deletions as compared to, to the amino acid sequence CSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDV PWNVVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTD VSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMV TLGNSFLHKLCSGFVRIX1IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTL DQSSEVLGSGKTLTIQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQK EPKNKTFLRCEAKNYSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVR GDNKEYEYSVECQEDSACPAAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQ LKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICR KNASISVRAQDRYYSSSWSEWASVPCSX2RNLPVATPDPGMFPCLHHSQNLLRAVSNML QKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLPLELTKNESCLNSRETSFITNGSCLASR KTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNF NSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS (SEQ ID NO.: 72), wherein X1is present or absent, and if present, is a linker having a length of from about 4 to about 16 amino acids and / or wherein the linker comprises a GlyxSery amino acid sequence, wherein, further optionally, the linker comprises, consists essentially of, or consists of the sequence GGGSGGGS (SEQ ID NO.: 7), and wherein X2 is a linker that optionally comprises a GlyxSery sequence and / or has a length of from about 10 to about 25 amino acids, preferably about 15 amino acids, wherein, further optionally, the linker comprises, consists essentially of, or consists of the sequence GGGGSGGGGSGGGGS (SEQ ID NO.: 8)); and / or (viii) the fusion protein comprises, consists essentially of, or consists of the amino acid sequence CSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDV PWNVVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTD VSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMV TLGNSFLHKLCSGFVRIGGGSGGGSIWELKKDVYVVELDWYPDAPGEMVVLTCDTPEE DGITWTLDQSSEVLGSGKTLTIQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWST DILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAAT LSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKP DPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKT SATVICRKNASISVRAQDRYYSSSWSEWASVPCSGGGGSGGGGSGGGGSRNLPVATPDP GMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLPLELTK NESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKR QIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRV MSYLNAS (SEQ ID NO.: 18); and / or (ix) the T cell or host cell further encodes or expresses, or the polynucleotide or expression construct further encodes, a CD8αβ co-receptor, or a functional portion or variant thereof (e.g., comprising a M1 isoform, and / or comprising a CD8β polypeptide and / or a CD8α polypeptide as described in PCT / US2021 / 063409 or in PCT / US2023 / 066048; and / or (x) the T cell or host cell further encodes or expresses, or the polynucleotide or expression construct further encodes, a CD4 co-receptor, or a functional portion or variant thereof; and / or (xi) the CBD comprises, consists essentially or, or consists of an amino acid sequence having at least 75%, at least 80%, 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity to, and / or comprises no more than 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 amino acid substitutions, deletions, and / or insertions relative to, any one or more of the amino acid sequences shown in Table 1. Embodiment 44. The polynucleotide of any one of Embodiments 12, 14-38, 42, and 43, wherein the polynucleotide comprises DNA. Embodiment 45. The polynucleotide of any one of Embodiments 12, 14-38 and 42- 44, wherein the polynucleotide comprises RNA, optionally mRNA. Embodiment 46. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of Embodiments 10, 11, and 14-43, the polynucleotide of any one of Embodiments 12 and 14-38 and 42-45, or the expression construct of any one of Embodiments 13, 15-38, 42, and 43, wherein the target-binding protein comprises a CAR, wherein, optionally, (1) the CAR is multispecific and is further optionally bispecific, and / or (2) the CAR comprises a binding domain that comprises any one or more of: an antibody heavy chain variable domain (VH), an antibody light chain variable domain (VL), a VH and a VL, a single-chain variable fragment (scFv) comprising VH-linker-VL or VL-linker-VH, a fragment antigen-binding region (Fab), a single-chain Fab, an antigen-binding fragment of a heavy chain-only antibody (VHH, also referred-to as a nanobody), a killer immunoreceptor from a NK cell, a VNAR, a designed ankyrin repeat protein (DARPin (Binz et al., J. Mol. Biol.332:489, 2003 and Binz et al., Nat. Biotechnol.22:575, 2004)), a FNIII domain such as an AdnectinTM or monobody ((Richards et al., J. Mol. Biol.326:1475, 2003; Parker et al., Protein Eng. Des. Selec.18:435, 2005 and Hackel et al. (2008) J. Mol. Biol.381:1238-1252, and Chandler and Buckle, Cells 9(2):610 (2020); doi: 10.3390 / cells9030610)), a lectin binding domain, a receptor ectodomain or functional portion or fragment thereof, a ligand such as e.g. a cytokine, a fully synthetic polypeptide (e.g. designed in silico, such as using the AlphaFold modeling program), a fibrinogen domain (see, e.g., Weisel et al., Science 230:1388, 1985), a Kunitz domain (see, e.g., US Patent No.6,423,498), a cysteine- knot miniprotein (Vita et al. (1995) Proc. Nat′l. Acad. Sci. (USA) 92:6404-6408; Martin et al. (2002) Nat. Biotechnol.21:71, 2002 and Huang et al. (2005) Structure 13:755, 2005; Lui et al. Nature Communications 11:295 (2020)), a tetratricopeptide repeat domain (Main et al., Structure 11:497, 2003 and Cortajarena et al., ACS Chem. Biol.3:161, 2008), a leucine-rich repeat domain (Stumpp et al., J. Mol. Biol.332:471, 2003), a lipocalin domain (see, e.g., WO 2006 / 095164, Beste et al., Proc. Nat′l. Acad. Sci. (USA) 96:1898, 1999 and Schönfeld et al., Proc. Nat′l. Acad. Sci. (USA) 106:8198, 2009), an armadillo repeat protein (see, e.g., Madhurantakam et al., Protein Sci.21: 1015, 2012; PCT Patent Application Publication No. WO 2009 / 040338), an affilin (Ebersbach et al., J. Mol. Biol.372: 172, 2007), an affibody, an avimer, a knottin, a fynomer, an atrimer, cytotoxic T-lymphocyte associated protein-4 (Weidle et al., Cancer Gen. Proteo.10:155, 2013) or the like (Nord et al., Protein Eng.8:601, 1995; Nord et al., Nat. Biotechnol.15:772, 1997; Nord et al., Euro. J. Biochem.268:4269, 2001; Binz et al., Nat. Biotechnol.23:1257, 2005; Boersma and Plückthun, Curr. Opin. Biotechnol.22:849, 2011), a centyrin, or the like. Embodiment 47. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of Embodiments 10, 11, and 14-43, the polynucleotide of any one of Embodiments 12 and 14-38 and 42-45, or the expression construct of any one of Embodiments 13, 15-38, 42, and 43, wherein the target-binding protein comprises a TCR, optionally an αβ TCR, further optionally a MHC Class I-restricted TCR or a MHC Class II-restricted TCR. Embodiment 48. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of Embodiments 10, 11, and 14-43, the polynucleotide of any one of Embodiments 12 and 14-38 and 42-45, or the expression construct of any one of Embodiments 13, 15-38, 42, and 43, wherein the target-binding protein comprises a scTCR, optionally, wherein the scTCR is multispecific, further optionally bispecific. Embodiment 49. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of Embodiments 10, 11, and 14-43, the polynucleotide of any one of Embodiments 12, 14-38, and 42-45, or the expression construct of any one of Embodiments 13, 15-38, 42, and 43, wherein the target-binding protein comprises a TCR / CAR, wherein, optionally, the TCR / CAR is multispecific, further optionally bispecific. Embodiment 50. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of Embodiments 10, 11, and 14-43, the polynucleotide of any one of Embodiments 12, 14-38, and 42-45, or the expression construct of any one of Embodiments 13, 15-38, 42, and 43, wherein the target-binding protein comprises an IFP, optionally, the IFP is multispecific, further optionally bispecific. Embodiment 51. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of Embodiments 10, 11, and 14-43, the polynucleotide of any one of Embodiments 12, 14-38, and 42-45, or the expression construct of any one of Embodiments 13, 15-38, 42, and 43, wherein the target-binding protein comprises a synNotch receptor, optionally, the synNotch receptor is multispecific, further optionally bispecific. Embodiment 52. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of Embodiments 10, 11, and 14-43, the polynucleotide of any one of Embodiments 12, 14-38, and 42-45, or the expression construct of any one of Embodiments 13, 15-38, 42, and 43, wherein the target-binding protein comprises a multispecific T cell engager (e.g., a BiTE that binds to an antigen and to a T cell surface protein, such as a CD3 protein). Embodiment 53. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-52, the host cell of any one of Embodiments 10, 11, and 14-52, the polynucleotide of any one of Embodiments 12, 14-38 and 42-52, or the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 46-52, wherein the target comprises: a target (e.g., an antigen) expressed by a cancer cell, a target (e.g., an antigen) associated with an autoimmune disease or disorder, a target (e.g., an antigen) associated with a neurological disease, a target (e.g., an antigen) associated with a neurodegenerative disease, a target (e.g., an antigen) associated with an aging-related disease, a viral antigen, a bacterial antigen, a fungal antigen, a parasitic antigen, a cytokine, a toxin, or a combination of any two or more of the foregoing. Embodiment 54. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, and 46-53, the host cell of any one of Embodiments 10, 11, and 14-53, the polynucleotide of any one of Embodiments 12, 14-38, and 42-53, or the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 46-53, wherein the target is an antigen that comprises or is from (e.g., human) STEAP1, ROR1, PNE, EGFR, GPRC5D, SLAMF7, EGFRvIII, EGP-2, EGP-40, GD2, GD3, GPC3, Claudin, B7-H3, HPV E6, HPV E7, HER2, L1-CAM, Lewis A, Lewis Y, MUC1, MUC16, MUC21, PSCA, PSMA, CA125, CA15-3, CA19-9, CD5, CD7, CD19, CD20, CD22, CD23, CD24, CD30, CD33, CD37, CD44v6, CD44v7 / 8, CD38, CD56, CD70, CD79b, CD87, CD123, CD152, CD200, CD229, CA125, c-MET, CCNA1, FcRH5, WT1, FAS, folate receptor α, human chorionic gonadotropin (hCG or beta-hCG), VEGF-α, VEGFR1, VEGFR2, IL-13Rα2, IL-11Rα, Igbeta, MAGE-A1, PSA, ephrin A2, ephrin B2, EpCAM, NKG2D, NY-ESO-1, T4, MMP2, BT-001, GUCY2C, TAG-72, TGFβ, mesothelin, TRBC1, FLT3, CLL1, SIGLEC-6, NY-ESO, 5T4, BCMA, FAP, Carbonic anhydrase 9, BRAF, α- fetoprotein (AFP), MAGE-A3, MAGE-A4, SSX-2, SOX2, OIP5, PBK, Core Binding Factor (CBF), a Merkel Cell Carcinoma antigen, TACI, PRAME, HA-1, β2M, ETA, EWS-FLI, tyrosinase, KRAS, p53, NRAS, HRAS, McPyV, CEA, CEACAM1, CEACAM6, CEACAM5, TREM2, CD71, alpha-synuclein, and / or an amyloid beta, or wherein the target comprises or is an MHC (e.g., HLA):antigen complex that comprises the antigen, or wherein the target comprises or is a label, such as FITC or a dinitrophenyl (DNP) such as 2,4-DNP, or a tag such as a Strep Tag (such as Strep-Tag or Strep-Tag II), a His Tag, a Myc Tag, a Flag Tag, or the like). Embodiment 55. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, and 46-54, the host cell of any one of Embodiments 10, 11, and 14-54, the polynucleotide of any one of Embodiments 12, 14-38, and 42-54, or the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 46-54, wherein the T cell or host cell encodes or express, or wherein the polynucleotide or expression construct encodes, two or more target-binding proteins, wherein the two or more target-binding proteins target different targets, wherein, optionally, the two or more target-binding proteins comprise: two or more CARs, two or more scTCRs, two or more multispecific T cell engagers, two or more TCRs, two or more IFPs, two or more synNotch receptors, two or more TCR / CARs, a CAR and a scTCR, a CAR and a multispecific T cell engager, a CAR and a TCR, a CAR and an IFP, a CAR and a synNotch receptor, a CAR and a TCR / CAR, a scTCR and a multispecific T cell engager, a multispecific T cell engager and an IFP, a multispecific T cell engager and a synNotch receptor, a TCR / CAR and a IFP, a TCR / CAR and a TCR, a TCR / CAR and a synNotch receptor, an IFP and a TCR, an IFP and a synNotch receptor, a scTCR and a TCR, a scTCR and an IFP, or a scTCR and a synNotch receptor. Embodiment 56. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, 45-54, the host cell of any one of Embodiments 10, 11, and 14-54, the polynucleotide of any one of Embodiments 12, 14-38, and 42-54, or the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 45-54, wherein the T cell or host cell encodes or expresses, or wherein the polynucleotide or expression construct encodes, two or more target-binding proteins, wherein the two or more target-binding proteins target different epitopes on the same target wherein, optionally, the two or more target-binding proteins comprise: two or more CARs, two or more scTCRs, two or more multispecific T cell engagers, two or more TCRs, two or more IFPs, two or more synNotch receptors, two or more TCR / CARs, a CAR and a scTCR, a CAR and a multispecific T cell engager, a CAR and a TCR, a CAR and an IFP, a CAR and a synNotch receptor, a CAR and a TCR / CAR, a scTCR and a multispecific T cell engager, a multispecific T cell engager and an IFP, a multispecific T cell engager and a synNotch receptor, a TCR / CAR and a IFP, a TCR / CAR and a TCR, a TCR / CAR and a synNotch receptor, an IFP and a TCR, an IFP and a synNotch receptor, a scTCR and a TCR, a scTCR and an IFP, or a scTCR and a synNotch receptor. Embodiment 57. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, 45-56, the host cell of any one of Embodiments 10, 11, and 14-56, the polynucleotide of any one of Embodiments 12, 14-38, and 42-56, or the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 45-56, wherein the target-binding protein is multispecific and binds to, or wherein the T cell or host cell encodes or expresses, or wherein the polynucleotide or expression construct encodes, two or more (e.g., monospecific) target-binding proteins and the two or more target-binding proteins bind to different targets, wherein, optionally, the different targets comprise: CD19 and CD20, respectively; CD19 and CD22, respectively; GD2 and CD70, respectively; GD2 and CD56, respectively; GD2 and PSMA, respectively; CD70 and PSMA, respectively; BCMA and CD19, respectively; BCMA and TACI, respectively; CD19, CD20, and CD22, respectively; BCMA and GPRC5D, respectively; CD19 and CD70, respectively; CD19 and CD79b, respectively; CD20 and CD22, respectively; CD20 and CD79b, respectively; CD33 and CLL1, respectively; BCMA and SLAMF7, respectively; BCMA and CD229, respectively; GPRC5D and SLAMF7, respectively; GPRC5D and CD229, respectively; SLAMF7 and CD229, respectively; EphA2 and IL-13Rα2, respectively; HER2 and MUC1, respectively; EGFR, EpCAM, and HER2, respectively; HER2 and IL-13Rα2, respectively; GD2 and B7H3, respectively; CEA and MSLN, respectively; or CD19 and CD229, respectively. Embodiment 58. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, 46-57, the host cell of any one of Embodiments 10, 11, and 14-57, the polynucleotide of any one of Embodiments 12, 14-38, and 42-57, or the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 46-57, wherein the target is an antigen expressed by cells of a hematological malignancy. Embodiment 59. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, 45-58, the host cell of any one of Embodiments 10, 11, and 14-58, the polynucleotide of any one of Embodiments 12, 14-38, and 42-58, or the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 45-58, wherein the target is an antigen expressed by cells of a solid tumor. Embodiment 60. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-59, the host cell of any one of Embodiments 10, 11, and 14-59, the polynucleotide of any one of Embodiments 12, 14-38, and 42-59, or the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 45-59, wherein the target-binding protein comprises an IFP, wherein, optionally, the target comprises: FasL, CD200, CD47, PVR aka CD155, TNF-α, a CSF (e.g., GM-CSF or G-CSF), PD-L1, PD-1, CD270 (HVEM), GAL9, CEACAM-1, phosphatidylserine (PtdSer), HMGB1, CTLA4, CD80, CD86, a B7-CD28 superfamily member, or combination of any two or more of the foregoing. Embodiment 61. A vector comprising the polynucleotide of any one of Embodiments 12, 14-38, and 42-60 or the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 45-60. Embodiment 62. The vector of Embodiment 61, which is a viral vector. Embodiment 63. The vector of Embodiment 62, which is a lentiviral vector. Embodiment 64. The vector of Embodiment 62, which is a retroviral vector, such as a γ-retroviral vector. Embodiment 65. The vector of Embodiment 62, which is an adeno-associated virus vector (AAV). Embodiment 66. The vector of Embodiment 62, which is derived from a baculovirus or an α-virus. Embodiment 67. The vector of Embodiment 61, which is a transposon vector. Embodiment 68. The vector of Embodiment 61, which is a Sleeping Beauty vector, a piggyBac vector, a mariner vector, a frog prince vector, a Tol2 vector, or a SPIN vector. Embodiment 69. The vector of any one of Embodiments 61-68, comprising the following features in 5’-->3’ orientation: (i) [5’LTR]-[optional one, two, three, four, five, six, or more NFAT binding sites]-[ promoter 1]-[gene 1]-[promoter 2]-[gene 2]-[3’LTR], wherein: promoter 1 is optionally a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; and 3’LTR is optionally a self-inactivating LTR; or (ii) [5’LTR]-[one, two, three, four, five, six, or more NFAT binding sites]- [optional promoter 1]-[gene 1]-[promoter 2]-[gene 2]-[3’LTR], wherein: optional promoter 1 is a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; and 3’LTR is optionally a self-inactivating LTR. Embodiment 70. The vector of any one of Embodiments 61-68, comprising the following features in 3’-->5’ orientation: (i) [3’ LTR]-[optional one to six NFAT binding sites]-[promoter 1]-[gene 1]- [polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]-[5’ LTR], wherein: promoter 1 is optionally a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; and 3’LTR is optionally a self-inactivating LTR; or (ii) [3’ LTR]-[one to six NFAT binding sites]-[optional promoter 1]-[gene 1]- [polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]-[5’ LTR], wherein: optional promoter 1 is a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; and 3’LTR is optionally a self-inactivating LTR. Embodiment 71. The vector of Embodiment 67, wherein the vector is a transposon vector, optionally a Sleeping Beauty vector or a piggyBac vector, and the vector comprises the following elements: (i) [3’ ITR]-[optional one to six NFAT binding sites]-[promoter 1]-[gene 1]- [polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]-[5’ ITR], wherein: each ITR is an inverted terminal repeat; promoter 1 is optionally a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target- binding protein and gene 2 encodes the fusion protein; (ii) [3’ ITR]-[one to six NFAT binding sites]-[optional promoter 1]-[gene 1]- [polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]-[5’ ITR], wherein: each ITR is an inverted terminal repeat; optional promoter 1 is a NFAT binding- inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; (iii) [3’ ITR]-[HS4 insulator]-[optional one to six NFAT binding sites]-[promoter 1]-[gene 1]-[polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]- [HS4 insulator]-[5’ ITR], wherein: each ITR is an inverted terminal repeat; promoter 1 is optionally a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target- binding protein and gene 2 encodes the fusion protein; (iv) [3’ ITR]-[HS4 insulator]-[one to six NFAT binding sites]-[optional promoter 1]-[gene 1]-[polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]- [HS4 insulator]-[5’ ITR], wherein: each ITR is an inverted terminal repeat; optional promoter 1 is a NFAT binding- inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; (v) [5’ ITR]-[optional one to six NFAT binding sites]-[promoter 1]-[gene 1]- [polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]-[3’ ITR], wherein: each ITR is an inverted terminal repeat; promoter 1 is optionally a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target- binding protein and gene 2 encodes the fusion protein; (vi) [5’ ITR]-[one to six NFAT binding sites]-[optional promoter 1]-[gene 1]- [polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]-[3’ ITR], wherein each ITR is an inverted terminal repeat; optional promoter 1 is a NFAT binding- inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; (vii) [5’ ITR]-[HS4 insulator] [optional one to six NFAT binding sites]-[promoter 1]-[gene 1]-[polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]- [HS4 insulator]-[3’ ITR], wherein each ITR is an inverted terminal repeat; promoter 1 is optionally a NFAT- inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; or (viii) [5’ ITR]-[HS4 insulator] [one to six NFAT binding sites]-[optional promoter 1]-[gene 1]-[polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]- [HS4 insulator]-[3’ ITR], wherein each ITR is an inverted terminal repeat; optional promoter 1 is a NFAT binding- inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein. Embodiment 72. A targeting polynucleotide construct comprising the polynucleotide of any one of Embodiments 12, 14-38, and 42-60 or the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 45-60, and: a splice acceptor; and / or a sequence encoding a self-cleaving peptide or a cleavage site; and / or a left homology arm homologous to a first portion of a target locus; and / or a polyA sequence; and / or a right homology arm homologous to a second portion of a target locus, wherein, optionally, the target locus comprises safe harbor locus, wherein, further optionally, the target locus is or comprises a (e.g., human) TRAC, TRBC, Rosa26, AAVS1, CCR5, CD8α, CD8β, CD4 (see, e.g., Xu et al., Cell Stem Cell 24(4):P566-587.E7 (2019), doi.org / 10.1016 / j.stem.2019.02.005), PDCD1 (PD1), TIGIT, LAG3, BTLA, CTLA4, HAVCR3 (TIM3), TNFRSF18 (GITR), CD47 (see, e.g., Yamada-Hunter et al., Nature (2024), doi.org / 10.1038 / s41586-024-07443-8), HLA-A, HLA-B, HLA-C, B2M, or CD40L locus. Embodiment 73. A kit or system comprising: the targeting polynucleotide construct of Embodiment 72; a guide RNA targeting a portion of the target locus; and a polynucleotide (e.g., mRNA) or vector (e.g., a viral vector) encoding a Cas protein (e.g., Cas9), or a Cas protein and optional amphilphilic peptides for delivery of the Cas protein (see, e.g., Voss et al., Nat Biomed Eng.2023 May;7(5):647-660. doi: 10.1038 / s41551-023-01032-2). Embodiment 74. A host cell comprising the polynucleotide of any one of Embodiments 12, 14-38, and 42-60, the expression construct of any one of Embodiments 13, 15- 38, 42, 43, and 46-60, the vector of any one of Embodiments 61-71, or the targeting polynucleotide construct of Embodiment 72, wherein, optionally, the host cell comprises a human cell, an immune system cell, a hematopoietic progenitor cell, a stem cell, a peripheral blood mononuclear cell (PBMC), or any combination thereof, wherein, further optionally, the host cell comprises a T cell, a NK cell, a NK-T cell, a dendritic cell, a macrophage, a B cell, a monocyte, or any combination thereof, wherein, even further optionally, the host cell comprises a CD4+ T cell, a CD8+ T cell, a CD4- CD8- double negative T cell, a γδ T cell, a naïve T cell, a central memory T cell, a stem cell memory T cell, an effector memory T cell, a tumor infiltrating lymphocyte (TIL), or any combination thereof. Embodiment 75. A cell population or composition comprising a plurality of the T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-60 and / or a plurality of the host cell of any one of Embodiments 10, 11, 14-59, and 74. Embodiment 76. A composition comprising: (1) the T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-60; the host cell of any one of Embodiments 10, 11, 14-59, and 74; the polynucleotide of any one of Embodiments 12, 14-38, and 42-60; the expression construct of any one of Embodiments 13, 15- 38, 42, 43, and 46-60; the vector of any one of Embodiments 61-71; the targeting polynucleotide construct of Embodiment 72; and / or the cell population or composition of Embodiment 75; and (2) a pharmaceutically acceptable carrier, excipient, or diluent, wherein, optionally: the composition comprises CD8+ T cells encoding or expressing the fusion protein and an antigen-specific MHC Class I-restricted TCR, and the composition further comprises CD4+ T cells encoding or expressing the antigen-specific MHC Class I-restricted TCR and a CD8αβ co- receptor polypeptide; and / or the composition comprises CD8+ T cells encoding or expressing the fusion protein and an antigen-specific CAR, and the composition further comprises CD4+ T cells encoding or expressing the antigen-specific CAR; and / or the composition comprises tumor infiltrating lymphocytes (TILs); and / or the composition further comprises a checkpoint inhibitor antibody or antigen-binding fragment thereof, wherein the checkpoint inhibitor antibody or antigen-binding fragment thereof optionally comprises an anti-PD1 antibody or antigen-binding fragment thereof, an anti-PD-L1 antibody or antigen-binding fragment thereof, an anti-CTLA4 antibody or antigen-binding fragment thereof, an anti-LAG3 antibody or antigen-binding fragment thereof, an anti-TIM3 antibody or antigen-binding fragment thereof, an anti-TIGIT antibody or antigen-binding fragment thereof, an anti-GITR antibody or antigen-binding fragment thereof, an anti-CD40 antibody or antigen-binding fragment thereof, an anti-CD137 antibody or antigen-binding fragment thereof, an anti-VISTA antibody or antigen-binding fragment thereof, an anti-CD47 antibody or antigen-binding fragment thereof, an anti-KIR antibody or antigen-binding fragment thereof, an anti-ICOS antibody or antigen-binding fragment thereof, an anti-CD20 antibody or antigen-binding fragment thereof, an anti-CD155 antibody or antigen-binding fragment thereof, an anti-PVRIG antibody or antigen-binding fragment thereof, an anti-B7-H4 antibody or antigen- binding fragment thereof, an anti-B7-H3 antibody or antigen-binding fragment thereof, an anti- CD244 / 2B4 antibody or antigen-binding fragment thereof, an anti-HVEM antibody or antigen- binding fragment thereof, an anti-BTLA antibody or antigen-binding fragment thereof, an anti- CD160 antibody or antigen-binding fragment thereof, an anti-GAL9 antibody or antigen-binding fragment thereof, an anti-PVRL3 antibody or antigen-binding fragment thereof, an anti-LAIR1 antibody or antigen-binding fragment thereof, an antibody or antigen-binding fragment that targets an immunosuppressive cytokine such as IL-10, IL-4, IL-1RA, or IL-35), an anti-IDO antibody or antigen-binding fragment thereof, an anti-CEACAM-1 antibody or antigen-binding fragment thereof, an anti-CEACAM-3 antibody or antigen-binding fragment thereof, an anti- CEACAM-5 antibody or antigen-binding fragment thereof, an antibody or antigen-binding fragment that targets Treg cells, an anti-adenosine antibody or antigen-binding fragment thereof, an anti-A2aR antibody or antigen-binding fragment thereof, or any combination of two or more of the foregoing. Embodiment 77. The composition of Embodiment 76, wherein the polynucleotide, expression construct, or targeting polynucleotide construct is comprised in a carrier, wherein the carrier comprises a lipid, a lipid-derived delivery vehicle, such as a liposome, a solid lipid nanoparticle, an oily suspension, a submicron lipid emulsion, a lipid microbubble, an inverse lipid micelle, a cochlear liposome, a lipid microtubule, a lipid microcylinder, lipid nanoparticle (LNP), a lipopolyplex (LPP), a cationic polypeptide, a polymeric nanoparticle, or a nanoscale platform, such as a nanoemulsion. Embodiment 78. A method comprising introducing into a host cell: the polynucleotide of any one of Embodiments 12, 14-38, and 42-60; the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 46-60; the vector of any one of Embodiments 61-71; the targeting polynucleotide construct of Embodiment 72, or the composition of Embodiment 76 or 77, wherein, optionally, (1) the host cell comprises a human cell, an immune system cell, a hematopoietic progenitor cell, a stem cell, a peripheral blood mononuclear cell (PBMC), or any combination thereof, wherein, further optionally, the host cell comprises a T cell, a NK cell, a NK-T cell, a dendritic cell, a macrophage, a monocyte, or any combination thereof, wherein, even further optionally, the host cell comprises a CD4+ T cell, a CD8+ T cell, a CD4- CD8- double negative T cell, a γδ T cell, a naïve T cell, a central memory T cell, a stem cell memory T cell, an effector memory T cell, a tumor infiltrating lymphocyte (TIL), or any combination thereof, and / or (2) the method is performed in vitro, in vivo, or ex vivo. Embodiment 79. A host cell made by the method of Embodiment 78. Embodiment 80. A method for treating a disease or disorder in a subject, the method comprising administering to the subject an effective amount of: the T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-60; the host cell of any one of Embodiments 10, 11, 14-60, 74, and 79; the polynucleotide of any one of Embodiments 12, 14-38, and 42-60; the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 46-60; the vector of any one of Embodiments 61-71; the targeting polynucleotide construct of Embodiment 72; the composition of Embodiment 76 or 77; and / or the cell population of Embodiment 75, wherein, optionally: the method comprises administering to the subject an effective amount of CD8+ T cells encoding or expressing the fusion protein and an antigen-specific MHC Class I-restricted TCR, and further administering to the subject an effective amount of CD4+ T cells encoding or expressing the antigen-specific MHC Class I-restricted TCR and a CD8αβ co-receptor polypeptide; and / or the method comprises administering to the subject an effective amount of CD8+ T cells encoding or expressing the fusion protein and an antigen-specific CAR, and further administering to the subject an effective amount of CD4+ T cells encoding or expressing the antigen-specific CAR; and / or the method further comprises administering to the subject an effective amount of a checkpoint inhibitor antibody or antigen-binding fragment thereof, wherein the checkpoint inhibitor antibody or antigen-binding fragment thereof optionally comprises an anti-PD1 antibody or antigen-binding fragment thereof (e.g., Opdivo® 240 mg every 2 weeks or 480 mg every 4 weeks), an anti-PD-L1 antibody or antigen-binding fragment thereof, an anti-CTLA4 antibody or antigen-binding fragment thereof, , an anti-LAG3 antibody or antigen-binding fragment thereof, an anti-TIM3 antibody or antigen-binding fragment thereof, an anti-TIGIT antibody or antigen-binding fragment thereof, an anti-GITR antibody or antigen-binding fragment thereof, an anti-CD40 antibody or antigen-binding fragment thereof, an anti-CD137 antibody or antigen-binding fragment thereof, an anti-VISTA antibody or antigen-binding fragment thereof, an anti-CD47 antibody or antigen-binding fragment thereof, an anti-KIR antibody or antigen-binding fragment thereof, an anti-ICOS antibody or antigen-binding fragment thereof, an anti-CD20 antibody or antigen-binding fragment thereof, an anti-CD155 antibody or antigen-binding fragment thereof, an anti-PVRIG antibody or antigen-binding fragment thereof, an anti-B7-H4 antibody or antigen-binding fragment thereof, an anti-B7-H3 antibody or antigen-binding fragment thereof, an anti-CD244 / 2B4 antibody or antigen-binding fragment thereof, an anti-HVEM antibody or antigen-binding fragment thereof, an anti-BTLA antibody or antigen-binding fragment thereof, an anti-CD160 antibody or antigen-binding fragment thereof, an anti-GAL9 antibody or antigen-binding fragment thereof, an anti-PVRL3 antibody or antigen-binding fragment thereof, an anti-LAIR1 antibody or antigen-binding fragment thereof, an antibody or antigen-binding fragment that targets an immunosuppressive cytokine such as IL-10, IL-4, IL-1RA, or IL-35), an anti-IDO antibody or antigen-binding fragment thereof, an anti-CEACAM-1 antibody or antigen-binding fragment thereof, an anti- CEACAM-3 antibody or antigen-binding fragment thereof, an anti-CEACAM-5 antibody or antigen-binding fragment thereof, an antibody or antigen-binding fragment that targets Treg cells, an anti-adenosine antibody or antigen-binding fragment thereof, an anti-A2aR antibody or antigen-binding fragment thereof, or any combination of two or more of the foregoing. Embodiment 81. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-60, the host cell of any one of Embodiments 10, 11, 14-60, 74, and 79, the polynucleotide of any one of Embodiments 12, 14-38, and 42-60, the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 46-60, the vector of any one of Embodiments 61-71, the targeting polynucleotide construct of Embodiment 72, the composition of Embodiment 76 or 77, and / or the cell population of Embodiment 75, for use in a method of treating a disease or disorder in a subject. Embodiment 82. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-60, the host cell of any one of Embodiments 10, 11, 14-60, 74, and 79, the polynucleotide of any one of Embodiments 12, 14-38, and 42-60, the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 46-60, the vector of any one of Embodiments 61-71, the targeting polynucleotide construct of Embodiment 72; the composition of Embodiment 76 or 77, and / or the cell population of Embodiment 75, for use in the manufacture of a medicament for treating a disease or disorder in a subject. Embodiment 83. The T cell of any one of Embodiments 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-60, the host cell of any one of Embodiments 10, 11, 14-60, 74, and 79, the polynucleotide of any one of Embodiments 12, 14-38, and 42-60, the expression construct of any one of Embodiments 13, 15-38, 42, 43, and 46-60, the vector of any one of Embodiments 61-71, the targeting polynucleotide construct of Embodiment 72; the composition of Embodiment 76 or 77, and / or the cell population of Embodiment 75, for use as a medicament. Embodiment 84. The method of Embodiment 80 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of any one of Embodiments 81-83, wherein the disease or disorder is selected from a hyperproliferative disease or disorder, a proliferative disease or disorder, an autoimmune disease or disorder, a neurodegenerative disease or disorder, a neurological disease or disorder, an aging-related disease or disorder, a bacterial infection, a viral infection, a fungal infection, and a parasitic infection. Embodiment 85. The method of Embodiment 84 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of Embodiment 84, wherein the disease or disorder comprises a cancer. Embodiment 86. The method of Embodiment 85 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of Embodiment 85, wherein the cancer is a hematologic malignancy. Embodiment 87. The method of Embodiment 85 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of Embodiment 85, wherein the cancer is a solid cancer. Embodiment 88. The method of Embodiment 85 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of Embodiment 85, wherein the cancer is selected from a carcinoma, a melanoma, a sarcoma, a glioma, a lymphoma, a leukemia, and a myeloma. Embodiment 89. The method of Embodiment 85 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of Embodiment 85, wherein the cancer comprises: a cancer of the head or neck, melanoma, pancreatic cancer, cholangiocarcinoma, hepatocellular cancer, breast cancer including triple-negative breast cancer (TNBC), gastric cancer, non-small-cell lung cancer, prostate cancer, esophageal cancer, mesothelioma, small-cell lung cancer, colorectal cancer, glioblastoma, Askin's tumor, sarcoma botryoides, chondrosarcoma, Ewing's sarcoma, PNET, malignant hemangioendothelioma, malignant schwannoma, osteosarcoma, alveolar soft part sarcoma, angiosarcoma, cystosarcoma phyllodes, dermatofibrosarcoma protuberans (DFSP), desmoid tumor, desmoplastic small round cell tumor, epithelioid sarcoma, extraskeletal chondrosarcoma, extraskeletal osteosarcoma, fibrosarcoma, gastrointestinal stromal tumor (GIST), hemangiopericytoma, hemangiosarcoma, Kaposi's sarcoma, leiomyosarcoma, liposarcoma, lymphangiosarcoma, lymphosarcoma, undifferentiated pleomorphic sarcoma, malignant peripheral nerve sheath tumor (MPNST), neurofibrosarcoma, rhabdomyosarcoma, synovial sarcoma, undifferentiated pleomorphic sarcoma, squamous cell carcinoma, basal cell carcinoma, adenocarcinoma, linitis plastic, vipoma, cholangiocarcinoma, hepatocellular carcinoma, adenoid cystic carcinoma, renal cell carcinoma, Grawitz tumor, ependymoma, astrocytoma, oligodendroglioma, brainstem glioma, optice nerve glioma, a mixed glioma, Hodgkin’s lymphoma, a B-cell lymphoma, non-Hodgkin’s lymphoma (NHL), Burkitt's lymphoma, acute lymphoblastic leukemia (ALL) small lymphocytic lymphoma (SLL), diffuse large B-cell lymphoma, follicular lymphoma (CL), immunoblastic large cell lymphoma, precursor B-lymphoblastic lymphoma, mantle cell lymphoma, Waldenström's macroglobulinemia, CD37+ dendritic cell lymphoma, lymphoplasmacytic lymphoma, splenic marginal zone lymphoma, extra-nodal marginal zone B cell lymphoma of mucosa-associated (MALT) lymphoid tissue, nodal marginal zone B-cell lymphoma, mediastinal (thymic) large B- cell lymphoma, intravascular large B-cell lymphoma, primary effusion lymphoma, adult T-cell lymphoma, extranodal NK / T-cell lymphoma, nasal type, enteropathy-associated T-cell lymphoma, hepatosplenic T-cell lymphoma, blastic NK cell lymphoma, Sezary syndrome, angioimmunoblastic T cell lymphoma, anaplastic large cell lymphoma, chronic lymphocytic leukemia (CLL), chronic myeloid leukemia, chondrosarcoma, fibrosarcoma (fibroblastic sarcoma), Dermatofibrosarcoma protuberans (DFSP), osteosarcoma, rhabdomyosarcoma, Ewing’s sarcoma, a gastrointestinal stromal tumor, Leiomyosarcoma, angiosarcoma (vascular sarcoma), Kaposi’s sarcoma, liposarcoma, pleomorphic sarcoma, synovial sarcoma, a lung carcinoma (e.g., Adenocarcinoma, Squamous Cell Carcinoma (Epidermoid Carcinoma), Squamous cell carcinoma, Adenocarcinoma, Adenosquamous carcinoma, anaplastic carcinoma; Large cell carcinoma, Small cell carcinoma, a breast carcinoma (e.g., Ductal Carcinoma in situ (non-invasive), Lobular carcinoma in situ (non-invasive), Invasive Ductal Carcinoma, Invasive lobular carcinoma, Non-invasive Carcinoma), a liver carcinoma (e.g., Hepatocellular Carcinoma, Cholangiocarcinomas or Bile Duct Cancer), Large-cell undifferentiated carcinoma, Bronchioalveolar carcinoma), an ovarian carcinoma (e.g., Surface epithelial-stromal tumor (Adenocarcinoma) or ovarian epithelial carcinoma (which includes serous tumor, endometrioid tumor and mucinous cystadenocarcinoma), Epidermoid (Squamous cell carcinoma), Embryonal carcinoma and choriocarcinoma (germ cell tumors)), a kidney carcinoma (e.g., Renal adenocarcinoma, hypernephroma, Transitional cell carcinoma (renal pelvis), Squamous cell carcinoma, Bellini duct carcinoma, Clear cell adenocarcinoma, Transitional cell carcinoma, Carcinoid tumor of the renal pelvis), an adrenal carcinoma (e.g., Adrenocortical carcinoma), a carcinoma of the testis (e.g., Germ cell carcinoma (Seminoma, Choriocarcinoma, Embryonal carciroma, Teratocarcinoma), Serous carcinoma), Gastric carcinoma (e.g., Adenocarcinoma), an intestinal carcinoma (e.g., Adenocarcinoma of the duodenum), a colorectal carcinoma, a skin carcinoma (e.g., Basal cell carcinoma, Squamous cell carcinoma), an ovarian carcinoma, an ovarian epithelial carcinoma, a cervical adenocarcinoma or small cell carcinoma, a pancreatic carcinoma, a colorectal carcinoma (e.g., an adenocarcinoma or squamous cell carcinoma), a lung carcinoma, a breast ductal carcinoma, Merkel Cell Carcinoma, and / or an adenocarcinoma of the prostate. Embodiment 90. The method of any one of Embodiments 80 and 84-89 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of Embodiment 84-89, wherein the subject is human. Embodiment 91. The method of any one of Embodiments 80 and 84-89 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of Embodiment 84-89, wherein the subject has not received or does not receive chemotherapy pre-conditioning (e.g., comprising fludarabine, cyclophosphamide, pentostatin, bendustamine, oxaliplatin, or any combination thereof). Embodiment 92. The method of any one of Embodiments 79, 80, and 84-91 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of Embodiment 84-91, wherein the cell is autologous to the subject, is allogeneic to the subject, or is produced in the subject. Embodiment 93. A kit comprising: (i) the T cell of any one of Embodiments 1, 11, 14-38, 42, 43, and 45-60; the host cell of any one of Embodiments 10, 11, 14-60, 74, and 79; the polynucleotide of any one of Embodiments 12, 14-38, and 42-60; the expression construct of any one of Embodiments 13, 15- 38, 42, 43, and 46-60; the vector of any one of Embodiments 61-71; the targeting polynucleotide construct of Embodiment 72; the composition of Embodiment 76 or 77; and / or the cell population of Embodiment 75; and any one or more of (ii)-(iv): (ii) a container for the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population; (iii) a means for delivering the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population into a subject (e.g., an intravenous delivery system, a syringe, or the like); (iv) instructions for delivering the polynucleotide, expression construct, vector, or targeting polynucleotide construct into a host cell, or for delivering the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population into a subject. Embodiment 94. A host cell, such as a T cell (optionally a human T cell) encoding or expressing a collagen-binding payload wherein the collagen-binding payload comprises a collagen-binding means linked or fused to a payload (e.g., a cytokine or a subunit thereof, a toxin, a polypeptide that inhibits an interaction between two or more proteins, an antibody or antigen-binding portion thereof, or a combination of any two or more of the foregoing. Embodiment 95. A host cell, such as a T cell (optionally a human T cell) encoding or expressing a collagen-binding payload wherein the collagen-binding payload comprises a collagen-binding polypeptide means linked or fused to a payload (e.g., a cytokine or a subunit thereof, a toxin, a polypeptide that inhibits an interaction between two or more proteins, an antibody or antigen-binding portion thereof, or a combination of any two or more of the foregoing. Embodiment 96. A host cell (e.g., a T cell, such as a human T cell) expressing or encoding (1) a target-binding means and (2) a collagen-binding means linked or fused to a payload. Embodiment 97. A polynucleotide, vector, expression construct, or targeting polynucleotide encodes (1) a target-binding means and (2) a collagen-binding means linked or fused to a payload. Embodiment 98. A(n, e.g., human) CD8+ T cell that encodes or expresses (i) a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the T cell encodes or expresses the cytokine; and (ii) a target-binding protein, wherein the target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR) that is optionally heterologous to the T cell, a single-chain TCR (scTCR), a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP). Embodiment 99. The CD8+ T cell of Embodiment 98, provided in a composition or combination with, administered with, or administered separately to as a combination cell therapy with CD4+ T cells, for example in about a 1:1 CD8+ to CD4+ ratio. The CD4+ T cells can encode or express: a target-binding protein (optionally, a target-binding protein that binds the same target as the target-binding protein of the CD8+ T cells, and further optionally, is the same target-binding protein as encoded or expressed by the CD8+ T cells); a CD8αβ co-receptor. Embodiment 100. A(n, e.g., human) CD8+ T cell that encodes or expresses (i) a fusion protein that comprises, consists essentially of, or consists of a collagen-binding means linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the T cell encodes or expresses the cytokine; and (ii) a target-binding means. Embodiment 101. The CD8+ T cell of Embodiment 100 provided in a composition with, administered with, or administered separately to as a combination cell therapy with CD4+ T cells, for example in about a 1:1 CD8+ to CD4+ ratio. Embodiment 102. The CD8+ T cell of Embodiment 101, wherein the CD4+ T cell encodes or expresses: a target-binding means (optionally, a target-binding means that binds the same target as the target-binding means of the CD8+ T cells, and further optionally, is the same target-binding means as encoded or expressed by the CD8+ T cells); a CD8αβ co-receptor, preferably wherein the CD8β chain is the M1 isoform and / or comprises a wild-type or mutant costimulatory domain from a human CD28 protein, e.g., as provided herein; and an IFP, optionally a CD200R:CD28 IFP or a Fas-4-1BB IFP. Embodiment 103. A polynucleotide, expression construct, or targeting polynucleotide that encodes: a target-binding protein that is capable of binding a peptide:MHC Class I complex; a CD8αβ co-receptor, preferably wherein the CD8β chain is the M1 isoform and / or comprises a wild-type or mutant costimulatory domain from a human CD28 protein, e.g., as provided herein; and an IFP, optionally a CD200R:CD28 IFP or a Fas-4-1BB IFP. Embodiment 104. A vector that comprises the polynucleotide, expression construct, or targeting polynucleotide of Embodiment 103. Embodiment 105. A(n, e.g., human) CD4+ T cell that comprises the polynucleotide, expression construct, targeting polynucleotide, or vector of Embodiment 103 or 104. Embodiment 106. A(n, e.g., human) CD4+ T cell that encodes expresses: a target- binding protein that is capable of binding a peptide:MHC Class I complex; a CD8αβ co-receptor, preferably wherein the CD8β chain is the M1 isoform and / or comprises a wild-type or mutant costimulatory domain from a human CD28 protein, e.g., as provided herein; and an IFP, optionally a CD200R:CD28 IFP or a Fas-4-1BB IFP. In preferred embodiments, the target- binding protein is a TCR, a scTCR, or a TCR-CAR. Embodiment 107. Use of any one or more of the preceding Embodiments in the treatment of a cancer in a human subject, optionally a solid cancer, further optionally prostate cancer, pancreas cancer, or breast cancer, still further optionally metastatic castration-reisstant prostate cancer. The following disclosure includes additional detail related to at least some of the foregoing Enumerated Embodiments, and includes additional embodiments that may, for example, be combined with the Enumerated Embodiments. In certain further embodiments, a polynucleotide comprises: (a) the polynucleotide encoding a polypeptide comprising an extracellular portion of a CD8 co-receptor α chain; (b) the polynucleotide encoding a polypeptide comprising an extracellular portion of a CD8 co-receptor β chain; and (c) a polynucleotide encoding a self-cleaving peptide disposed between the polynucleotide of (a) and the polynucleotide of (b). In further embodiments, a polynucleotide comprises a polynucleotide that encodes a self-cleaving peptide and is disposed between: (1) the polynucleotide encoding a target-binding protein and the polynucleotide encoding a polypeptide comprising an extracellular portion of a CD8 co-receptor α chain; and / or (2) the polynucleotide encoding a binding protein and the polynucleotide encoding a polypeptide comprising an extracellular portion of a CD8 co-receptor β chain. In any of the presently disclosed embodiments, a self-cleaving peptide can comprise a linker N-terminal and / or C-terminal to the self-cleaving (e.g., viral 2A) sequence. Non-limiting examples of linkers include GSG, GPP, PGP, and AAA. In still further embodiments, a polynucleotide can comprise, operably linked in-frame: (i) (pnCD8α)-(pnSCP1)-(pnCD8β)-(pnSCP2)-(pnBP); (ii) (pnCD8β)-(pnSCP1)-(pnCD8α)- (pnSCP2)-(pnBP); (iii) (pnBP)-(pnSCP1)-(pnCD8α)-(pnSCP2)-(pnCD8β); (iv) (pnBP)-(pnSCP1)-(pnCD8β)-(pnSCP2)-(pnCD8α); (v) (pnCD8α)-(pnSCP1)-(pnBP)- (pnSCP2)-(pnCD8β); or (vi) (pnCD8β)-(pnSCP1)-(pnBP)-(pnSCP2)-(pnCD8α), wherein pnCD8α is the polynucleotide encoding a polypeptide that comprises an extracellular portion of a CD8 co-receptor α chain, wherein pnCD8β is the polynucleotide encoding a polypeptide that comprises an extracellular portion of a CD8 co-receptor α chain, wherein pnBP is the polynucleotide encoding a target-binding protein, and wherein pnSCP1 and pnSCP2 are each independently a polynucleotide encoding a self-cleaving peptide, wherein the polynucleotides and / or the encoded self-cleaving peptides are optionally the same or different (e.g., P2A, T2A, F2A, E2A, optionally comprising a linker disposed N-terminal and / or C-terminal of the 2A sequence). In certain embodiments, the encoded binding protein comprises a TCRα chain and a TCRβ chain, wherein the polynucleotide comprises a polynucleotide encoding a self-cleaving peptide disposed between the polynucleotide encoding a TCRα chain and the polynucleotide encoding a TCRβ chain. In further embodiments, the polynucleotide comprises, operably linked in-frame: (i) (pnCD8α)-(pnSCP1)-(pnCD8β)-(pnSCP2)-(pnTCRβ)-(pnSCP3)-(pnTCRα); (ii) (pnCD8β)-(pnSCP1)-(pnCD8α)-(pnSCP2)-(pnTCRβ)-(pnSCP3)-(pnTCRα); (iii) (pnCD8α)-(pnSCP1)-(pnCD8β)-(pnSCP2)-(pnTCRα)-(pnSCP3)-(pnTCRβ); (iv) (pnCD8β)-(pnSCP1)-(pnCD8α)-(pnSCP2)-(pnTCRα)-(pnSCP3)-(pnTCRβ); (v) (pnTCRβ)-(pnSCP1)-(pnTCRα)-(pnSCP2)-(pnCD8α)-(pnSCP3)-(pnCD8β); (vi) (pnTCRβ)-(pnSCP1)-(pnTCRα)-(pnSCP2)-(pnCD8β)-(pnSCP3)-(pnCD8α); (vii) (pnTCRα)-(pnSCP1)-(pnTCRβ)-(pnSCP2)-(pnCD8α)-(pnSCP3)-(pnCD8β); (viii) (pnTCRα)- (pnSCP1)-(pnTCRβ)-(pnSCP2)-(pnCD8β)-(pnSCP3)-(pnCD8α), wherein pnCD8α is the polynucleotide encoding a polypeptide that comprises an extracellular portion of a CD8 co- receptor α chain, wherein pnCD8β is the polynucleotide encoding a polypeptide that comprises an extracellular portion of a CD8 co-receptor α chain, wherein pnTCRα is the polynucleotide encoding a TCR α chain, wherein pnTCRβ is the polynucleotide encoding a TCR β chain, and wherein pnSCP1, pnSCP2, and pnSCP3 are each independently a polynucleotide encoding a self- cleaving peptide, wherein the polynucleotides and / or the encoded self-cleaving peptides are optionally the same or different. In certain embodiments, an encoded polypeptide of the present disclosure comprises one or more junction amino acids. "Junction amino acids" or "junction amino acid residues" refer to one or more (e.g., 2 to about 10) amino acid residues between two adjacent motifs, regions, or domains of a polypeptide, such as between a binding domain and an adjacent constant domain or between a TCR chain and an adjacent self-cleaving peptide. Junction amino acids can result from the design of a construct that encodes a fusion protein (e.g., amino acid residues resulting from the use of a restriction enzyme site during the construction of a nucleic acid molecule encoding a fusion protein), or from cleavage of, for example, a self-cleaving peptide adjacent one or more domains of an encoded binding protein of this disclosure (e.g., a P2A peptide disposed between a TCR α-chain and a TCR β-chain, the self-cleavage of which can leave one or more junction amino acids in the α-chain, the TCR β-chain, or both). In further embodiments, a binding protein is expressed as part of a transgene construct that encodes, and / or a host cell of the present disclosure can encode: one or more additional accessory protein, such as a safety switch protein; a tag, a selection marker; a CD8 co receptor β chain; a CD8 co-receptor α chain or both; or any combination thereof. Polynucleotides and transgene constructs useful for encoding and expressing binding proteins and accessory components (e.g., one or more of a safety switch protein, a selection marker, CD8 co-receptor β- chain, or a CD8 co-receptor α-chain) are described in PCT application PCT / US2017 / 053112, the polynucleotides, transgene constructs, and accessory components, including the nucleotide and amino acid sequences, of which are hereby incorporated by reference. It will be understood that any or all of a binding protein of the present disclosure, a safety switch protein, a tag, a selection marker, a CD8 co-receptor β chain, or a CD8 co-receptor α-chain may be encoded by a single nucleic acid molecule or may be encoded by polynucleotide sequences that are, or are present on, separate nucleic acid molecules. Exemplary safety switch proteins include, for example, a truncated EGF receptor polypeptide (huEGFRt) that is devoid of extracellular N terminal ligand binding domains and intracellular receptor tyrosine kinase activity, but that retains its native amino acid sequence, has type I transmembrane cell surface localization, and has a conformationally intact binding epitope for pharmaceutical-grade anti-EGFR monoclonal antibody, cetuximab (Erbitux) tEGF receptor (tEGFr; Wang et al., Blood 118:1255-1263, 2011); a caspase polypeptide (e.g., iCasp9; Straathof et al., Blood 105:4247-4254, 2005; Di Stasi et al., N. Engl. J. Med.365:1673-1683, 2011; Zhou and Brenner, Exp. Hematol. pii:S0301-472X(16)30513-6. doi:10.1016 / j.exphem.2016.07.011), RQR8 (Philip et al., Blood 124:1277-1287, 2014); a 10-amino-acid tag derived from the human c-myc protein (Myc) (Kieback et al., Proc. Natl. Acad. Sci. USA 105:623-628, 2008); and a marker / safety switch polypeptide, such as RQR (CD20 + CD34; Philip et al., 2014). Other accessory components useful for modified host cells of the present disclosure comprise a tag or selection marker that allows the cells to be identified, sorted, isolated, enriched, or tracked. For example, marked host cells having desired characteristics (e.g., an antigen-specific TCR and a safety switch protein) can be sorted away from unmarked cells in a sample and more efficiently activated and expanded for inclusion in a product of desired purity. As used herein, the term "selection marker" comprises a nucleic acid construct (and the encoded gene product) that confers an identifiable change to a cell permitting detection and positive selection of immune cells transduced with a polynucleotide comprising a selection marker. RQR is a selection marker that comprises a major extracellular loop of CD20 and two minimal CD34 binding sites. In some embodiments, an RQR-encoding polynucleotide comprises a polynucleotide that encodes the 16-amino-acid CD34 minimal epitope. In some embodiments, the CD34 minimal epitope is incorporated at the amino terminal position of a CD8 co-receptor stalk domain (Q8). In further embodiments, the CD34 minimal binding site sequence can be combined with a target epitope for CD20 to form a compact marker / suicide gene for T cells (RQR8) (Philip et al., 2014, incorporated by reference herein). This construct allows for the selection of host cells expressing the construct, with for example, CD34 specific antibody bound to magnetic beads (Miltenyi) and that utilizes clinically accepted pharmaceutical antibody, rituximab, that allows for the selective deletion of a transgene expressing engineered T cell (Philip et al., 2014). Further exemplary selection markers also include several truncated type I transmembrane proteins normally not expressed on T cells: the truncated low-affinity nerve growth factor, truncated CD19, and truncated CD34 (see for example, Di Stasi et al., N. Engl. J. Med. 365:1673-1683, 2011; Mavilio et al., Blood 83:1988-1997, 1994; Fehse et al., Mol. Ther.1:448- 456, 2000; each incorporated herein in their entirety). A useful feature of CD19 and CD34 is the availability of the off-the-shelf Miltenyi CliniMACsTM selection system that can target these markers for clinical-grade sorting. However, CD19 and CD34 are relatively large surface proteins that may tax the vector packaging capacity and transcriptional efficiency of an integrating vector. Surface markers containing the extracellular, non signaling domains or various proteins (e.g., CD19, CD34, LNGFR) also can be employed. Any selection marker may be employed and should be acceptable for Good Manufacturing Practices. In certain embodiments, selection markers are expressed with a polynucleotide that encodes a gene product of interest (e.g., a binding protein of the present disclosure, such as a TCR or CAR). Further examples of selection markers include, for example, reporters such as GFP, EGFP, β-gal or chloramphenicol acetyltransferase (CAT). In certain embodiments, a selection marker, such as, for example, CD34 is expressed by a cell and the CD34 can be used to select enrich for, or isolate (e.g., by immunomagnetic selection) the transduced cells of interest for use in the methods described herein. As used herein, a CD34 marker is distinguished from an anti-CD34 antibody, or, for example, a scFv, TCR, or another antigen recognition moiety that binds to CD34. In certain embodiments, a selection marker comprises an RQR polypeptide, a truncated low-affinity nerve growth factor (tNGFR), a truncated CD19 (tCD19), a truncated CD34 (tCD34), or any combination thereof. Regarding RQR polypeptides, without wishing to be bound by theory, it is believed that distance from the host cell surface is important for RQR polypeptides to function as selection markers / safety switches (Philip et al., 2010 (supra)). In some embodiments, the encoded RQR polypeptide is contained in a β-chain, an α-chain, or both, or a fragment or variant of either or both, of the encoded CD8 co-receptor. In specific embodiments, a modified host cell comprises a heterologous polynucleotide encoding iCasp9 and a heterologous polynucleotide encoding a recombinant CD8 co-receptor protein that comprises a β chain containing a RQR polypeptide and further comprises a CD8 α-chain. An encoded CD8 co-receptor includes, in some embodiments, an α-chain or a fragment or variant thereof. An amino acid sequence of the human CD8 co-receptor α-chain precursor is known and is provided at, for example, UniProtKB –P30433 (see also UniProtKB – P31783; - P10732; and -P10731). An encoded CD8 co-receptor includes, in some embodiments, a β-chain or a fragment or variant thereof. An amino acid sequence of the human CD8 co-receptor β-chain precursor is known and is provided at, for example, UniProtKB –P10966 (see also UniProtKB – Q9UQ56; -E9PD41; Q8TD28; and -P30434; and -P05541). An isolated polynucleotide of this disclosure may further comprise a polynucleotide encoding a safety switch protein, a selection marker, a CD8 co-receptor beta chain, or a CD8 co- receptor alpha chain as disclosed herein, or may comprise a polynucleotide encoding any combination thereof. In any of the presently disclosed embodiments, a polynucleotide can be codon optimized for expression in a host cell. In some embodiments, the host cell comprises a human immune system cell, such as a T cell, a NK cell, or a NK-T cell (Scholten et al., Clin. Immunol.119:135, 2006). Codon optimization can be performed using known techniques and tools, e.g., using the GenScript® OptimumGeneTM tool, or GeneArt® (Life Technologies). Codon-optimized sequences include sequences that are partially codon-optimized (i.e., one or more of the codons is optimized for expression in the host cell) and those that are fully codon-optimized. It will be appreciated that in embodiments wherein a polynucleotide encodes more than one polypeptide (e.g., a TCR α chain, a TCR β chain, a CD8 co-receptor α chain, a CD8 co-receptor β chain, and one or more self-cleaving peptides), each polypeptide can independently fully codon optimized, partially codon optimized, or not codon optimized. Vectors In another aspect, the present disclosure provides an expression vector, comprising any polynucleotide as provided herein operably linked to an expression control sequence. Also provided herein are vectors that comprise a polynucleotide or transgene construct of the instant disclosure. Some examples of vectors include plasmids, viral vectors, cosmids, and others. Some vectors may be capable of autonomous replication in a host cell into which they are introduced (e.g., bacterial vectors having a bacterial origin of replication and episomal mammalian vectors), whereas other vectors may be integrated into the genome of a host cell or promote integration of the polynucleotide insert upon introduction into the host cell and thereby replicate along with the host genome (e.g., lentiviral vector, retroviral vector). Additionally, some vectors are capable of directing the expression of genes to which they are operably linked (these vectors may be referred to as "expression vectors"). According to related embodiments, it is further understood that, if one or more agents (e.g., polynucleotides encoding polypeptides as described herein) are co-administered to a subject, that each agent may reside in separate or the same vectors, and multiple vectors (each containing a different agent or the same agent) may be introduced to a cell or cell population or administered to a subject. In certain embodiments, polynucleotides of the present disclosure may be operably linked to certain elements of a vector. For example, polynucleotide sequences that are needed to effect the expression and processing of coding sequences to which they are ligated may be operably linked. Expression control sequences may include appropriate transcription initiation, termination, promoter, and enhancer sequences; efficient RNA processing signals such as splicing and polyadenylation signals; sequences that stabilize cytoplasmic mRNA; sequences that enhance translation efficiency (i.e., Kozak consensus sequences); sequences that enhance protein stability; and sequences that enhance protein secretion. Expression control sequences may be operably linked if they are contiguous with the gene of interest and expression control sequences that act in trans or at a distance to control the gene of interest. In certain embodiments, the vector comprises a plasmid vector or a viral vector (e.g., a vector selected from lentiviral vector or a γ-retroviral vector). Viral vectors include retrovirus, adenovirus, parvovirus (e.g., adeno-associated viruses), coronavirus, negative strand RNA viruses such as ortho-myxovirus (e.g., influenza virus), rhabdovirus (e.g., rabies and vesicular stomatitis virus), paramyxovirus (e.g., measles and Sendai), positive strand RNA viruses such as picornavirus and alphavirus, and double-stranded DNA viruses including adenovirus, herpesvirus (e.g., Herpes Simplex virus types 1 and 2, Epstein-Barr virus, cytomega¬lovirus), and poxvirus (e.g., vaccinia, fowlpox and canarypox). Other viruses include Norwalk virus, togavirus, flavivirus, reoviruses, papovavirus, hepadnavirus, and hepatitis virus, for example. Examples of retroviruses include avian leukosis-sarcoma, mammalian C-type, B-type viruses, D type viruses, HTLV-BLV group, lentivirus, and spumavirus (Coffin, J. M., Retroviridae: The viruses and their replication, In Fundamental Virology, Third Edition, B. N. Fields et al., Eds., Lippincott-Raven Publishers, Philadelphia, 1996). "Retroviruses" are viruses having an RNA genome, which is reverse-transcribed into DNA using a reverse transcriptase enzyme, the reverse-transcribed DNA is then incorporated into the host cell genome. "Gammaretrovirus" refers to a genus of the retroviridae family. Examples of gammaretroviruses include mouse stem cell virus, murine leukemia virus, feline leukemia virus, feline sarcoma virus, and avian reticuloendotheliosis viruses. "Lentiviral vector," as used herein, means lentiviral vectors for gene delivery, which can be integrative or non-integrative, have relatively large packaging capacity, and can transduce a range of different cell types. Lentiviral vectors are usually generated following transient transfection of three (packaging, envelope, and transfer) or more plasmids into producer cells. Like HIV, lentiviral vectors enter the target cell through the interaction of viral surface glycoproteins with receptors on the cell surface. On entry, the viral RNA undergoes reverse transcription, which is mediated by the viral reverse transcriptase complex. The product of reverse transcription is a double- stranded linear viral DNA, which is the substrate for viral integration into the DNA of infected cells. In some embodiments, a lentiviral vector is a self-inactivating lentiviral vector. A self- inactivating lentiviral vector can comprise a modification to prevent the transfer of enhancer and promoter elements in the 5' long terminal repeat (LTR) of the vector to transduced cells, for example, comprising a deletion in the 3'LTR of the viral genome that is transferred into the 5'LTR after one round of reverse transcription, resulting in a provirus that contains no LTR derived enhancer or promoter elements. In some embodiments, a lentiviral vector is a third generation lentiviral vector. A third generation lentiviral vector can utilize a packaging system split into two or more plasmids, e.g., one encoding Rev and one encoding Gag and Pol. A third generation lentiviral vector can utilize a packaging system that lacks Tat or does not require Tat expression, and instead comprises, e.g., a chimeric 5' LTR fused to a heterologous promoter on the transfer plasmid. In certain embodiments, the viral vector can be a gammaretrovirus, e.g., Moloney murine leukemia virus (MLV)-derived vectors. In other embodiments, the viral vector can be a more complex retrovirus-derived vector, e.g., a lentivirus-derived vector. HIV-1-derived vectors belong to this category. Other examples include lentivirus vectors derived from HIV-2, FIV, equine infectious anemia virus, SIV, and Maedi-Visna virus (ovine lentivirus). Methods of using retroviral and lentiviral viral vectors and packaging cells for transducing mammalian host cells with viral particles containing TCR or CAR transgenes are known in the art and have been previous described, for example, in: U.S. Patent 8,119,772; Walchli et al., PLoS One 6:327930, 2011; Zhao et al., J. Immunol.174:4415, 2005; Engels et al., Hum. Gene Ther.14:1155, 2003; Frecha et al., Mol. Ther.18:1748, 2010; and Verhoeyen et al., Methods Mol. Biol.506:97, 2009. Retroviral and lentiviral vector constructs and expression systems are also commercially available. Other viral vectors also can be used for polynucleotide delivery including DNA viral vectors, including, for example adenovirus-based vectors and adeno-associated virus (AAV)- based vectors; vectors derived from herpes simplex viruses (HSVs), including amplicon vectors, replication-defective HSV and attenuated HSV (Krisky et al., Gene Ther.5:1517, 1998). Other vectors developed for gene therapy uses can also be used with the compositions and methods of this disclosure. Such vectors include those derived from baculoviruses and α- viruses. (Jolly, D J.1999. Emerging Viral Vectors. pp 209-40 in Friedmann T. ed. The Development of Human Gene Therapy. New York: Cold Spring Harbor Lab), or plasmid vectors (such as Sleeping Beauty or other transposon vectors). When a viral vector genome comprises a plurality of polynucleotides to be expressed in a host cell as separate transcripts, the viral v...

Claims

1. CLAIMS What is claimed is:

1. A T cell encoding or expressing: (i) a fusion protein that comprises, consists essentially of, or consists of a collagen- binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the T cell encodes or expresses the cytokine; and (ii) a target-binding protein, wherein the target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR) that is optionally heterologous to the T cell, a single-chain TCR (scTCR), a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP).

2. A host cell encoding or expressing a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the host cell encodes or expresses the cytokine, and wherein the host cell comprises a T cell.

3. The T cell of claim 1 or the host cell of claim 2, wherein the T cell comprises a human T cell.

4. The T cell of claim 1 or 3 or the host cell of claim 2 or 3, wherein the T cell comprises a CD4+ T cell, a CD8+ T cell, a CD4- CD8- double negative T cell, a γδ T cell, a naïve T cell, a central memory T cell, a stem cell memory T cell, an effector memory T cell, or any combination thereof.

5. The T cell of claim 4 or the host cell of claim 4, wherein the T cell comprises a CD8+ T cell, a CD4+ T cell, or both.

6. A host cell encoding or expressing a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the host cell encodes or expresses the cytokine, and wherein the host cell comprises a human cell.

7. A host cell encoding or expressing a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the host cell encodes or expresses the cytokine, and wherein the host cell comprises a hematopoietic progenitor cell, a stem cell, a peripheral blood mononuclear cell (PBMC), a tumor infiltrating lymphocyte (TIL), or any combination thereof.

8. A host cell encoding or expressing a fusion protein that comprises, consists essentially of, or consists of a collagen-binding domain (CBD) linked to or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the host cell encodes or expresses the cytokine, wherein the host cell comprises an immune system cell, optionally comprising a T cell, a NK cell, a NK-T cell, a dendritic cell, a macrophage, a B cell, a monocyte, or any combination thereof.

9. The host cell of claim 7 or 8, wherein the host cell is a human cell.

10. The host cell of any one of claims 2-9, wherein the host cell further encodes or expresses a target-binding protein, wherein the target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR) that is optionally heterologous to the host cell, a single-chain TCR, a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP).

11. The T cell of claim 1, 3, 4, or 5, or the host cell of claim 10, wherein the target- binding protein is encoded by a polynucleotide or expression construct that also encodes the fusion protein and wherein, optionally, (1) a nucleotide sequence encoding the fusion protein is operably linked to a promoter, wherein, further optionally, (1) the promoter comprises a NFAT binding site and / or is an inducible promoter responsive to NFAT binding to a NFAT binding site and the polynucleotide or expression construct comprises one, two, three, four, five, six, or more NFAT binding sites, one or more of which is operably linked to the inducible promoter, and / or (2) a nucleotide sequence encoding the target-binding protein is operably linked to a constitutive promoter.

12. A polynucleotide encoding (i) a cytokine, wherein at least a portion (e.g., a subunit) of the cytokine is linked to or is directly fused to a collagen-binding domain (CBD), forming a fusion protein, and (ii) a target-binding protein, wherein the target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR), a single-chain TCR, a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP), wherein, optionally: (1) the polynucleotide is codon-optimized for expression in a human T cell; and / or (2) the polynucleotide comprises a promoter operably linked to a nucleotide sequence encoding the target-binding protein, wherein, further optionally, the promoter comprises a constitutive promoter; and / or (3) the polynucleotide comprises a promoter operably linked to a nucleotide sequence encoding the cytokine or a portion thereof, wherein, optionally, the promoter comprises a NFAT binding site and / or is an inducible promoter responsive to NFAT binding to a NFAT binding site and the polynucleotide comprises one, two, three, four, five, six, or more NFAT binding sites, one or more of which is operably linked to the inducible promoter; and / or (4) the cytokine comprises a plurality of subunits, the polynucleotide encodes each of the plurality of subunits, and one or more of the plurality of subunits is linked or is directly fused to one or more CBD, further optionally wherein, between nucleotide sequences encoding the plurality of subunits, are nucleotide sequences that each independently encode a cleavage sequence (e.g., 2A self-cleaving peptide sequence, furin cleavage site) and / or comprise an IRES.

13. An expression construct comprising a promoter operably linked to a nucleotide sequence encoding a fusion protein that comprises, consists essentially of, or consists of: a collagen-binding domain (CBD) linked or directly fused to a cytokine or a portion thereof (e.g., to a subunit of the cytokine), wherein the promoter comprises a NFAT binding site and / or is an inducible promoter operably linked to one or more NFAT binding sites of the expression construct, wherein, optionally, (1) a NFAT-binding site comprises, consists essentially of, or consists of the nucleotide sequence Ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 20), and / or the expression construct comprises two, three, four, five, six, or more NFAT-binding sites, wherein, further optionally, each of the two, three, four, five, six, or more NFAT-binding sites comprises, consists essentially of, or consists of the nucleotide sequence Ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 20), wherein, even further optionally, the expression construct comprises the following nucleotide sequence: Ggaggaaaaactgtttcatacagaaggcgtggaggaaaaactgtttcatacagaaggcgtggaggaaaaactgtttcatacagaaggcgt ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 21), and / or (2) the promoter comprises, consists essentially of, or consists of the nucleotide sequence tagagggtatataatggaagctcgatttccag (SEQ ID NO.: 22); and / or (3) the cytokine comprises a plurality of subunits, the expression vector encodes each of the plurality of subunits, and one or more of the plurality of subunits is linked or is directly fused to one or more CBD, further optionally wherein, between nucleotide sequences encoding the plurality of subunits, are nucleotide sequences that each independently encode a cleavage sequence (e.g., 2A self-cleaving peptide sequence, furin cleavage site, or the like) and / or comprise an IRES; and / or (4) the expression construct further encodes a target-binding protein, wherein the target-binding protein comprises a chimeric antigen receptor (CAR), a T cell receptor (TCR), a single-chain TCR, a TCR / CAR, a synNotch receptor, a multispecific T cell engager (e.g., a BiTE), a TRuC, or an immunomodulatory fusion protein (IFP), wherein a nucleotide sequence encoding the target-binding protein is operably linked to a promoter, wherein, further optionally, the promoter is a constitutive promoter and / or is a SFFV, PGK, EF1-alpha, CAG, MNDU3, CMV, CMV + intron, EFS, CBA, MSCV, MNDU3, SV40, mPGK, hPGK, UBC or CBh promoter.

14. The T cell of claim 1, 3, 4, 5, or 11, the host cell of any one of claims 2-11, or the polynucleotide of claim 12, wherein a promoter comprises a NFAT binding site and / or is operably linked to one or more NFAT binding site, the promoter being operably linked to a polynucleotide encoding the fusion protein, wherein, optionally, (1) an NFAT-binding site comprises, consists essentially of, or consists of the nucleotide sequence Ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 20), and / or the expression construct comprises two, three, four, five, six, or more NFAT-binding sites, wherein, further optionally, each of the two, three, four, five, six, or more NFAT-binding sites comprises, consists essentially of, or consists of the nucleotide sequence Ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 20), wherein, even further optionally, the expression construct comprises the following nucleotide sequence: Ggaggaaaaactgtttcatacagaaggcgtggaggaaaaactgtttcatacagaaggcgtggaggaaaaactgtttcatacagaaggcgt ggaggaaaaactgtttcatacagaaggcgt (SEQ ID NO.: 21), and / or (2) the promoter comprises, consists essentially of, or consists of the nucleotide sequence tagagggtatataatggaagctcgatttccag (SEQ ID NO.: 22), and / or (3) a nucleotide sequence encoding the target-binding protein is operably linked to a promoter, wherein, further optionally, the promoter is a constitutive promoter and / or is a SFFV, PGK, EF1-alpha, CAG, MNDU3, CMV, CMV + intron, EFS, CBA, MSCV, MNDU3, SV40, mPGK, hPGK, UBC or CBh promoter.

15. The T cell of any one of claims 1, 3, 4, 5, 11, and 14, the host cell of any one of claims 2-11 and 14, the polynucleotide of claim 12 or 14, or the expression construct of claim 13, wherein the fusion protein comprises a single CBD.

16. The T cell of claim 15, the host cell of claim 15, the polynucleotide of claim 15, or the expression construct of claim 15, wherein the single CBD is linked to or is directly fused to an amino-terminal end of the cytokine or a portion thereof.

17. The T cell of claim 15, the host cell of claim 15, the polynucleotide of claim 15, or the expression construct of claim 15, wherein the single CBD is linked to or is directly fused to a carboxy-terminal end of the cytokine or a portion thereof.

18. The T cell of any one of claims 1, 3, 4, 5, 11, and 14, the host cell of any one of claims 2-11 and 14, the polynucleotide of claim 12 or 14, or the expression construct of claim 13, wherein the fusion protein comprises two CBDs, wherein the two CBDs are the same or are different, and wherein the fusion protein optionally comprises only two CBDs, further optionally wherein the only two CBDs are the same.

19. The T cell of claim 18, the host cell of claim 18, the polynucleotide of claim 18, or the expression construct of claim 18, wherein the fusion protein comprises one CDB linked to or directly fused to an amino-terminal end of the cytokine or a portion thereof and one CBD linked to or directly fused to a carboxy-terminal end of the cytokine or a portion thereof.

20. The T cell of any one of claims 1, 3, 4, 5, 11, and 14-19, the host cell of any one of claims 2-11 and 14-19, the polynucleotide of any one of claims 12 and 14-19, or the expression construct of any one of claims 13 and 15-19, wherein the fusion protein comprises a CBD linked to the cytokine or a portion thereof by a linker, wherein, optionally, the linker has a length of from about 4 to about 16 amino acids and / or wherein the linker comprises a GlyxSery amino acid sequence, wherein, further optionally, the linker comprises, consists essentially of, or consists of the amino acid sequence GGGSGGGS (SEQ ID NO.: 7).

21. The T cell of any one of claims 1, 3, 4, 5, 11, and 14-20, the host cell of any one of claims 2-11 and 14-20, the polynucleotide of any one of claims 12 and 14-20, or the expression construct of any one of claims 13 and 15-20, wherein the fusion protein comprises a CBD directly fused to the cytokine or a portion thereof, wherein, optionally, a CBD is directly fused to an amino-terminal end of the cytokine or a portion thereof, and / or a CBD is directly fused to a carboxy-terminal end of the cytokine or a portion thereof.

22. The T cell of claim 18 or 19, the host cell of claim 18 or 19, the polynucleotide of claim 18 or 19, or the expression construct of claim 18 or 19, wherein the fusion protein comprises two CBDs, wherein one CBD is linked to an amino-terminal end of the cytokine or a portion thereof by a first linker and one CBD is linked to a carboxy-terminal end of the cytokine or a portion thereof by a second linker, wherein the first linker and the second linker are the same or are different.

23. The T cell of claim 18 or 19, the host cell of claim 18 or 19, the polynucleotide of claim 18 or 19, or the expression construct of claim 18 or 19, wherein the fusion protein comprises two CBDs, wherein one CBD is linked to the cytokine or a portion thereof by a linker and one CBD is directly fused to the cytokine or a portion thereof.

24. The T cell of claim 18 or 19, the host cell of claim 18 or 19, the polynucleotide of claim 18 or 19, or the expression construct of claim 18 or 19, wherein the fusion protein comprises two CBDs, wherein each of the two CBDs is directly fused to the cytokine or a portion thereof , optionally one CBD being directly fused to an amino-terminal end of the cytokine or a portion thereof and one CBD being directly fused to a carboxy-terminal end of the cytokine or a portion thereof.

25. The T cell of any one of claims 1, 3, 4, 5, 11, and 14-24, the host cell of any one of claims 2-11 and 14-24, the polynucleotide of any one of claims 12 and 14-24, or the expression construct of any one of claims 13 and 15-24, wherein the cytokine is an proinflammatory cytokine.

26. The T cell of any one of claims 1, 3, 4, 5, 11, and 14-24, the host cell of any one of claims 2-11 and 14-24, the polynucleotide of any one of claims 12 and 14-24, or the expression construct of any one of claims 13 and 15-24, wherein the cytokine comprises any one or more of, or is selected from: IL-12, IL-1, IL-2, IL-3, IL-4, IL-5, IL-6, IL-7, IL-8, IL-9, IL-10, IL-11, IL-13, IL-14, IL-15, IL-16, IL-17, IL-18, IL-19, IL-20, IL-21, IL-22, IL-23, IL-24, IL-25, IL-26, IL-27, IL-28, IL-29, IL-30, IL-31, IL-32, IL-33, IL-34, IL-35, IL-36, IL-37, IL-38, IL-39, TNF-α, TNF-β, IFNα, IFNβ, IFNγ, CCL1, CCL2, CCL3, CCL4, CCL5, CCL7, CCL8, CCL9, CCL10, CCL11, CCL12, CCL13, CCL14, CCL15, CCL16, CCL17, CCL18, CCL19, CCL20, CCL21, CXCL1, CXCL2 ,CXCL3, CXCL4, CXCL5, CXCL6, CXCL7, CXCL8, CXCL9, CXCL10, CXCL11, CXCL12, CXCL13, CXCL14, CXCL15, CXCL16, CXCL17, GM-CSF, G- CSF, TRAIL, FASL, and a functional portion or variant of any of the foregoing, or wherein the cytokine has at least 90% at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% amino acid sequence identity, similarity, and / or homology to a human: IL-12, IL-1, IL-2, IL-3, IL-4, IL-5, IL-6, IL-7, IL-8, IL-9, IL-10, IL-11, IL-13, IL-14, IL-15, IL-16, IL-17, IL-18, IL-19, IL-20, IL-21, IL-22, IL-23, IL-24, IL-25, IL-26, IL-27, IL-28, IL-29, IL-30, IL-31, IL-32, IL-33, IL-34, IL-35, IL-36, IL-37, IL-38, IL-39, TNF-α, TNF-β, IFNα, IFNβ, IFNγ, CCL1, CCL2, CCL3, CCL4, CCL5, CCL7, CCL8, CCL9, CCL10, CCL11, CCL12, CCL13, CCL14, CCL15, CCL16, CCL17, CCL18, CCL19, CCL20, CCL21, CXCL1, CXCL2 ,CXCL3, CXCL4, CXCL5, CXCL6, CXCL7, CXCL8, CXCL9, CXCL10, CXCL11, CXCL12, CXCL13, CXCL14, CXCL15, CXCL16, CXCL17, GM-CSF, G- CSF, TRAIL, or FASL.

27. The T cell of any one of claims 1, 3, 4, 5, 11, and 14-26, the host cell of any one of claims 2-11 and 14-26, the polynucleotide of any one of claims 12 and 14-26, or the expression construct of any one of claims 13 and 15-26, wherein the cytokine is a human cytokine or is derived from a human cytokine.

28. The T cell of any one of claims 1, 3, 4, 5, 11, and 14-27, the host cell of any one of claims 2-11 and 14-27, the polynucleotide of any one of claims 12 and 14-27, or the expression construct of any one of claims 13 and 15-27, wherein the cytokine comprises a plurality of subunits and two or more of the plurality of subunits are linked to or are directly fused to one another in a fusion protein.

29. The T cell of any one of claims 1, 3, 4, 5, 11, and 14-28, the host cell of any one of claims 2-11 and 14-28, the polynucleotide of any one of claims 12 and 14-28, or the expression construct of any one of claims 13 and 15-28, wherein the cytokine comprises an (e.g., human) IL-12, a TNFα, an IL-7, a CCL4, and / or an IFNγ.

30. The T cell of any one of claims 1, 3, 4, 5, 11, and 14-29, the host cell of any one of claims 2-11 and 14-29, the polynucleotide of any one of claims 12 and 14-29, or the expression construct of any one of claims 13 and 15-29, wherein the cytokine comprises a plurality of subunits, wherein a first subunit and a second subunit are linked by a linker or are directly fused to one another.

31. The T cell of any one of claims 1, 3, 4, 5, 11, and 14-30, the host cell of any one of claims 2-11 and 14-30, the polynucleotide of any one of claims 12 and 14-30, or the expression construct of any one of claims 13 and 15-30, wherein the cytokine comprises a plurality of subunits, wherein each of the plurality of subunits is linked or is to directly fused to another of the plurality of subunits.

32. The T cell of any one of claims 1, 3, 4, 5, 11, and 14-31, the host cell of any one of claims 2-11 and 14-31, the polynucleotide of any one of claims 12 and 14-31, or the expression construct of any one of claims 13 and 15-31, wherein the cytokine comprises an IL- 12, preferably a human IL-12.

33. The T cell of claim 32, the host cell of claim 32, the polynucleotide of claim 32, or the expression construct of claim 32, wherein a p40 subunit of the IL-12 is fused or linked directly to a CBD and / or wherein a p35 subunit of the IL-12 is fused or directly linked to a CBD.

34. The T cell of claim 32 or 33, the host cell of claim 32 or 33, the polynucleotide of claim 32 or 33, or the expression construct of claim 32 or 33, wherein a p40 subunit of the IL-12 is linked to a p35 subunit of the IL-12 to form a fusion protein (single-chain IL-12 or scIL-12), optionally wherein a linker links a C-terminal end of the p40 subunit to a N-terminal end of the p35 subunit.

35. The T cell of any one of claims 32-34, the host cell of any one of claims 32-34, the polynucleotide of any one of claims 32-34, or the expression construct of any one of claims 32-34, wherein a nucleotide sequence encoding a p40 subunit of the IL-12 is disposed 5’ of a nucleotide sequence encoding a p35 subunit of the IL-12.

36. The T cell of any one of claims 32-34, the host cell of any one of claims 32-34, the polynucleotide of any one of claims 32-34, or the expression construct of any one of claims 32-34, wherein a nucleotide sequence encoding a p40 subunit of the IL-12 is disposed 3’ of a nucleotide sequence encoding a p35 subunit of the IL-12.

37. The T cell of any one of claims 1, 3, 4, 5, 11, and 14-36, the host cell of any one of claims 2-11 and 14-36, the polynucleotide of any one of claims 12 and 14-36, or the expression construct of any one of claims 13 and 15-36, wherein the cytokine and / or the fusion protein comprises a linker, wherein the linker comprises, consists essentially of, or consists of any one or more of: a glycine-serine linker (e.g., (GlyxSery)n, wherein x, y, and n are each independently an integer selected from 1 to 10); a proline-glycine linker; an elastin or elastin-like linker (e.g., comprising or consisting of the sequence (VPGXG)n (SEQ ID NO.: 62), wherein X is any amino acid other than proline, and n represents the number of pentapeptide repeats, such as for example an integer selected from 1, 2, 3, 4, 5, and 6, or an integer from 1 to 5, or an integer from 1 to 6); a Whitlow linker (GSTSGSGKPGSGEGSTKG (SEQ ID NO.: 63)); a Townsend linker (GSGGSGGSGGTG (SEQ ID NO.: 64)); a linker comprising, consisting essentially of, or consisting of the sequence GSGKPGSGEG (SEQ ID NO.: 65); a linkercomprising, consisting essentially of, or consisting of the sequence GKPGSGEG (SEQ ID NO.: 66); SGKPGSGE (SEQ ID NO.: 67); a linker comprising, consisting essentially of, or consisting of a sequence BPXXXZ (SEQ ID NO.: 68), wherein each X is independently a glycine (G) or serine (S), B is a positively charged amino acid and Z is glycine (G) or a negatively charged amino acid; a linker comprising, consisting essentially of, or consisting of the sequence GSTSGGGSGGGSGGGGSS (SEQ ID NO.: 69); a linker comprising, consisting essentially of, or consisting of the sequence EGKSSGSGSESKVD (SEQ ID NO.: 70).

38. The T cell of any one of claims 32-37, the host cell of any one of claims 32-37, the polynucleotide of any one of claims 32-37, or the expression construct of any one of claims 32-37, wherein the IL-12 comprises a single chain fusion protein (scIL-12) wherein a p40 subunit of an optionally human IL-12, or a functional fragment or variant thereof, is linked by a linker to a p35 subunit of an optionally human IL-12, or a functional variant or fragment thereof, wherein: the scIL-12 comprises, in amino-terminal to carboxy-terminal direction: the p40 subunit, or a functional fragment or variant thereof; the linker; and the p35 subunit, or a functional fragment or variant thereof; and / or the linker comprises a (GlyxSery)n sequence, wherein x, y, and n are each independently an integer selected from 1 to 10, and / or has a length of from about 10 to about 25 amino acids, preferably about 15 amino acids, wherein, further optionally, the linker comprises, consists essentially of, or consists of the sequence GGGGSGGGGSGGGGS (SEQ ID NO.: 8); and / or the linker comprises any one or more of: a proline-glycine linker; an elastin or elastin-like linker (e.g., comprising or consisting of the sequence (VPGXG)n (SEQ ID NO.: 62), wherein X is any amino acid other than proline, and n represents the number of pentapeptide repeats, such as for example an integer selected from 1, 2, 3, 4, 5, and 6, or an integer from 1 to 5, or an integer from 1 to 6); a Whitlow linker (GSTSGSGKPGSGEGSTKG (SEQ ID NO.: 63)); a Townsend linker (GSGGSGGSGGTG (SEQ ID NO.: 64)); a linker comprising, consisting essentially of, or consisting of the sequence GSGKPGSGEG (SEQ ID NO.: 65); a linker comprising, consisting essentially of, or consisting of the sequence GKPGSGEG (SEQ ID NO.: 66); SGKPGSGE (SEQ ID NO.: 67); a linker comprising, consisting essentially of, or consisting of a sequence BPXXXZ (SEQ ID NO.: 68), wherein each X is independently a glycine (G) or serine (S), B is a positively charged amino acid and Z is glycine (G) or a negatively chargedamino acid; a linker comprising, consisting essentially of, or consisting of the sequence GSTSGGGSGGGSGGGGSS (SEQ ID NO.: 69); a linker comprising, consisting essentially of, or consisting of the sequence EGKSSGSGSESKVD (SEQ ID NO.: 70).

39. A host cell encoding or expressing a fusion protein comprising (i) a collagen- binding domain (CBD) and (ii) a payload portion, wherein the host cell comprises a human cell, a human immune cell, a tumor infiltrating lymphocyte (TIL), a hematopoietic progenitor cell, a stem cell, a peripheral blood mononuclear cell (PBMC), a T cell, a NK cell, a NK-T cell, a macrophage, a monocyte, a dendritic cell, a B cell, or any combination thereof, and wherein, optionally, the payload portion comprises an antibody or an antigen-binding fragment thereof, a cytokine, a toxin, a polypeptide that inhibits an interaction between two or more proteins, a detectable agent such as a tag or a fluorescent marker, or any combination thereof.

40. The host cell of claim 39, wherein the T cell comprises a CD4+ T cell, a CD8+ T cell, a CD4- CD8- double negative T cell, a γδ T cell, a naïve T cell, a central memory T cell, a stem cell memory T cell, an effector memory T cell, or any combination thereof.

41. The host cell of claim 40, wherein the T cell comprises a CD8+ T cell, a CD4+ T cell, or both.

42. The T cell of any one of claims 1, 3, 4, 5, 11, and 14-38, the host cell of any one of claims 2-11 and 14-41, the polynucleotide of any one of claims 12 and 14-38, or the expression construct of any one of claims 13 and 15-38, wherein the / a CBD comprises a CBD from or derived from: a von Willebrand Factor (vWF) A3 domain; a vWF A1 domain; a decorin; a lumican; a fibronectin; a placental growth factor (PlGF), such as PlGF1 or PlGF2; a collagen- binding peptide (e.g., comprising, consisting essentially of, or consisting of the amino acid sequence TKKTLRT (SEQ ID NO.: 48), and / or comprising, consisting essentially of, or consisting of the amino acid sequence LRELHLNNN (SEQ ID NO.: 49) and / or comprising, consisting essentially of, or consisting of the amino acid sequence WREPFSMALS (SEQ ID NO.: 50)), a bacterial surface protein (e.g., lipoprotein SLR, M protein, or M-like protein); a collagen mimetic peptide (CMP); an avimer; an antibody or antigen-binding fragment thereof; or a combination of any two or more of the foregoing.

43. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38 and 42, the host cell of any one of claims 2-11 and 14-42, the polynucleotide of any one of claims 12, 14-38 and 42, or the expression construct of any one of claims 13 and 15-38 and 42, wherein: (i) the fusion protein comprises a CBD that has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity or homology or similarity to, and / or comprises one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, or twenty amino acid substitutions, insertions, and / or deletions as compared to, to the amino acid sequence CSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDV PWNVVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTD VSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMV TLGNSFLHKLCSGFVRI (SEQ ID NO.: 5); and / or (ii) the CBD comprises, consists essentially of, or consists of the amino acid sequence CSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNV VPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTDVSVD SVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMVTLGN SFLHKLCSGFVRI (SEQ ID NO.: 5); (iii) the fusion protein comprises a p40 subunit of a human IL-12, or a functional portion or variant thereof that has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity or homology or similarity to, and / or comprises one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, or twenty amino acid substitutions, insertions, and / or deletions as compared to, to the amino acid sequence IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLT IQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKN YSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQE DSACPAAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSW EYPDTWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYS SSWSEWASVPCS (SEQ ID NO.: 3); and / or(iv) the fusion protein comprises a p35 subunit of a human IL-12, or a functional portion or variant thereof that has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity or homology or similarity to, and / or comprises one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, or twenty amino acid substitutions, insertions, and / or deletions as compared to, to the amino acid sequence RNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKD KTSTVEACLPLELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEF KTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCIL LHAFRIRAVTIDRVMSYLNAS (SEQ ID NO.: 4); and / or (v) fusion protein comprises an amino acid sequence that has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity or homology or similarity to, and / or comprises one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, or twenty amino acid substitutions, insertions, and / or deletions as compared to, to the amino acid sequence IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLT IQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKN YSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQE DSACPAAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSW EYPDTWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYS SSWSEWASVPCSXRNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEI DHEDITKDKTSTVEACLPLELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYED LKMYQVEFKTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDF YKTKIKLCILLHAFRIRAVTIDRVMSYLNAS (SEQ ID NO.: 71), wherein X is present or absent and, if present, is a linker that optionally comprises a (GlyxSery)n sequence and / or has a length of from about 10 to about 25 amino acids, preferably about 15 amino acids, wherein, further optionally, the linker comprises, consists essentially of, or consists of the sequence GGGGSGGGGSGGGGS (SEQ ID NO.: 8); and / or(vi) the fusion protein comprises the amino acid sequence IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKE FGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRF TCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACP AAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPD TWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWS EWASVPCSXRNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHED ITKDKTSTVEACLPLELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMY QVEFKTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKI KLCILLHAFRIRAVTIDRVMSYLNAS (SEQ ID NO.: 71), wherein X is present or absent and, if present, is a linker that optionally comprises a GlyxSery sequence and / or has a length of from about 10 to about 25 amino acids, preferably about 15 amino acids, wherein, further optionally, the linker comprises, consists essentially of, or consists of the sequence GGGGSGGGGSGGGGS (SEQ ID NO.: 8); and / or (vii) the fusion protein comprises, consists essentially of, or consists of an amino acid sequence that has at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% identity or homology or similarity to, and / or comprises one, two, three, four, five, six, seven, eight, nine, ten, eleven, twelve, thirteen, fourteen, fifteen, sixteen, seventeen, eighteen, nineteen, or twenty amino acid substitutions, insertions, and / or deletions as compared to, to the amino acid sequence CSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDV PWNVVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTD VSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMV TLGNSFLHKLCSGFVRIX1IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTL DQSSEVLGSGKTLTIQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQK EPKNKTFLRCEAKNYSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVR GDNKEYEYSVECQEDSACPAAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQ LKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICR KNASISVRAQDRYYSSSWSEWASVPCSX2RNLPVATPDPGMFPCLHHSQNLLRAVSNML QKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLPLELTKNESCLNSRETSFITNGSCLASR KTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS (SEQ ID NO.: 72), wherein X1is present or absent, and if present, is a linker having a length of from about 4 to about 16 amino acids and / or wherein the linker comprises a GlyxSery amino acid sequence, wherein, further optionally, the linker comprises, consists essentially of, or consists of the sequence GGGSGGGS (SEQ ID NO.: 7), and wherein X2 is a linker that optionally comprises a GlyxSery sequence and / or has a length of from about 10 to about 25 amino acids, preferably about 15 amino acids, wherein, further optionally, the linker comprises, consists essentially of, or consists of the sequence GGGGSGGGGSGGGGS (SEQ ID NO.: 8)); and / or (viii) the fusion protein comprises, consists essentially of, or consists of the amino acid sequence CSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDV PWNVVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTD VSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMV TLGNSFLHKLCSGFVRIGGGSGGGSIWELKKDVYVVELDWYPDAPGEMVVLTCDTPEE DGITWTLDQSSEVLGSGKTLTIQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWST DILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAAT LSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKP DPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKT SATVICRKNASISVRAQDRYYSSSWSEWASVPCSGGGGSGGGGSGGGGSRNLPVATPDP GMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLPLELTK NESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKR QIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRV MSYLNAS (SEQ ID NO.: 18); and / or (ix) the T cell or host cell further encodes or expresses, or the polynucleotide or expression construct further encodes, a CD8αβ co-receptor, or a functional portion or variant thereof (e.g., comprising a M1 isoform, and / or comprising a CD8β polypeptide and / or a CD8α polypeptide as described in PCT / US2021 / 063409 or in PCT / US2023 / 066048; and / or (x) the T cell or host cell further encodes or expresses, or the polynucleotide or expression construct further encodes, a CD4 co-receptor, or a functional portion or variant thereof; and / or (xi) the CBD comprises, consists essentially or, or consists of an amino acid sequence having at least 75%, at least 80%, 85%, at least 86%, at least 87%, at least 88%, at least 89%, atleast 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% identity, and / or comprises no more than 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 amino acid substitutions, deletions, and / or insertions relative to any one or more of the amino acid sequences shown in Table 1.

44. The polynucleotide of any one of claims 12, 14-38, 42, and 43, wherein the polynucleotide comprises DNA.

45. The polynucleotide of any one of claims 12, 14-38 and 42-44, wherein the polynucleotide comprises RNA, optionally mRNA.

46. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of claims 10, 11, and 14-43, the polynucleotide of any one of claims 12 and 14-38 and 42-45, or the expression construct of any one of claims 13, 15-38, 42, and 43, wherein the target- binding protein comprises a CAR, wherein, optionally, (1) the CAR is multispecific and is further optionally bispecific, and / or (2) the CAR comprises a binding domain that comprises any one or more of: an antibody heavy chain variable domain (VH), an antibody light chain variable domain (VL), a VH and a VL, a single-chain variable fragment (scFv) comprising VH-linker-VL or VL-linker-VH, a fragment antigen-binding region (Fab), a single-chain Fab, an antigen- binding fragment of a heavy chain-only antibody (VHH, also referred-to as a nanobody), a killer immunoreceptor from a NK cell, a VNAR, a designed ankyrin repeat protein (DARPin (Binz et al., J. Mol. Biol.332:489, 2003 and Binz et al., Nat. Biotechnol.22:575, 2004)), a FNIII domain such as an AdnectinTM or monobody ((Richards et al., J. Mol. Biol.326:1475, 2003; Parker et al., Protein Eng. Des. Selec.18:435, 2005 and Hackel et al. (2008) J. Mol. Biol.381:1238-1252, and Chandler and Buckle, Cells 9(2):610 (2020); doi: 10.3390 / cells9030610)), a lectin binding domain, a receptor ectodomain or functional portion or fragment thereof, a ligand such as e.g. a cytokine, a fully synthetic polypeptide (e.g. designed in silico, such as using the AlphaFold modeling program), a fibrinogen domain (see, e.g., Weisel et al., Science 230:1388, 1985), a Kunitz domain (see, e.g., US Patent No.6,423,498), a cysteine-knot miniprotein (Vita et al. (1995) Proc. Nat′l. Acad. Sci. (USA) 92:6404-6408; Martin et al. (2002) Nat. Biotechnol. 21:71, 2002 and Huang et al. (2005) Structure 13:755, 2005; Lui et al. Nature Communications 11:295 (2020)), a tetratricopeptide repeat domain (Main et al., Structure 11:497, 2003 andCortajarena et al., ACS Chem. Biol.3:161, 2008), a leucine-rich repeat domain (Stumpp et al., J. Mol. Biol.332:471, 2003), a lipocalin domain (see, e.g., WO 2006 / 095164, Beste et al., Proc. Nat′l. Acad. Sci. (USA) 96:1898, 1999 and Schönfeld et al., Proc. Nat′l. Acad. Sci. (USA) 106:8198, 2009), an armadillo repeat protein (see, e.g., Madhurantakam et al., Protein Sci.21: 1015, 2012; PCT Patent Application Publication No. WO 2009 / 040338), an affilin (Ebersbach et al., J. Mol. Biol.372: 172, 2007), an affibody, an avimer, a knottin, a fynomer, an atrimer, cytotoxic T-lymphocyte associated protein-4 (Weidle et al., Cancer Gen. Proteo.10:155, 2013) or the like (Nord et al., Protein Eng.8:601, 1995; Nord et al., Nat. Biotechnol.15:772, 1997; Nord et al., Euro. J. Biochem.268:4269, 2001; Binz et al., Nat. Biotechnol.23:1257, 2005; Boersma and Plückthun, Curr. Opin. Biotechnol.22:849, 2011), a centyrin, or the like.

47. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of claims 10, 11, and 14-43, the polynucleotide of any one of claims 12 and 14-38 and 42-45, or the expression construct of any one of claims 13, 15-38, 42, and 43, wherein the target- binding protein comprises a TCR, optionally an αβ TCR, further optionally a MHC Class I- restricted TCR or a MHC Class II-restricted TCR.

48. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of claims 10, 11, and 14-43, the polynucleotide of any one of claims 12 and 14-38 and 42-45, or the expression construct of any one of claims 13, 15-38, 42, and 43, wherein the target- binding protein comprises a scTCR, optionally, wherein the scTCR is multispecific, further optionally bispecific.

49. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of claims 10, 11, and 14-43, the polynucleotide of any one of claims 12, 14-38, and 42- 45, or the expression construct of any one of claims 13, 15-38, 42, and 43, wherein the target- binding protein comprises a TCR / CAR, wherein, optionally, the TCR / CAR is multispecific, further optionally bispecific.

50. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of claims 10, 11, and 14-43, the polynucleotide of any one of claims 12, 14-38, and 42- 45, or the expression construct of any one of claims 13, 15-38, 42, and 43, wherein the target-binding protein comprises an IFP, optionally, the IFP is multispecific, further optionally bispecific.

51. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of claims 10, 11, and 14-43, the polynucleotide of any one of claims 12, 14-38, and 42- 45, or the expression construct of any one of claims 13, 15-38, 42, and 43, wherein the target- binding protein comprises a synNotch receptor, optionally, the synNotch receptor is multispecific, further optionally bispecific.

52. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, and 43, the host cell of any one of claims 10, 11, and 14-43, the polynucleotide of any one of claims 12, 14-38, and 42- 45, or the expression construct of any one of claims 13, 15-38, 42, and 43, wherein the target- binding protein comprises a multispecific T cell engager (e.g., a BiTE that binds to an antigen and to a T cell surface protein, such as a CD3 protein).

53. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-52, the host cell of any one of claims 10, 11, and 14-52, the polynucleotide of any one of claims 12, 14-38 and 42-52, or the expression construct of any one of claims 13, 15-38, 42, 43, and 46-52, wherein the target comprises: a target (e.g., an antigen) expressed by a cancer cell, a target (e.g., an antigen) associated with an autoimmune disease or disorder, a target (e.g., an antigen) associated with a neurological disease, a target (e.g., an antigen) associated with a neurodegenerative disease, a target (e.g., an antigen) associated with an aging-related disease, a viral antigen, a bacterial antigen, a fungal antigen, a parasitic antigen, a cytokine, a toxin, or a combination of any two or more of the foregoing.

54. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, 43, and 46-53, the host cell of any one of claims 10, 11, and 14-53, the polynucleotide of any one of claims 12, 14-38, and 42-53, or the expression construct of any one of claims 13, 15-38, 42, 43, and 46-53, wherein the target is an antigen that comprises or is from (e.g., human) STEAP1, ROR1, PNE, EGFR, GPRC5D, SLAMF7, EGFRvIII, EGP-2, EGP-40, GD2, GD3, GPC3, Claudin, B7-H3, HPV E6, HPV E7, HER2, L1-CAM, Lewis A, Lewis Y, MUC1, MUC16, MUC21, PSCA, PSMA, CA125, CA15-3, CA19-9, CD5, CD7, CD19, CD20, CD22, CD23, CD24, CD30, CD33,CD37, CD44v6, CD44v7 / 8, CD38, CD56, CD70, CD79b, CD87, CD123, CD152, CD200, CD229, CA125, c-MET, CCNA1, FcRH5, WT1, FAS, folate receptor α, human chorionic gonadotropin (hCG or beta-hCG), VEGF-α, VEGFR1, VEGFR2, IL-13Rα2, IL-11Rα, Igbeta, MAGE-A1, PSA, ephrin A2, ephrin B2, EpCAM, NKG2D, NY-ESO-1, T4, MMP2, BT-001, GUCY2C, TAG-72, TGFβ, mesothelin, TRBC1, FLT3, CLL1, SIGLEC-6, NY-ESO, 5T4, BCMA, FAP, Carbonic anhydrase 9, BRAF, α-fetoprotein (AFP), MAGE-A3, MAGE-A4, SSX- 2, SOX2, OIP5, PBK, Core Binding Factor (CBF), a Merkel Cell Carcinoma antigen, TACI, PRAME, HA-1, β2M, ETA, EWS-FLI, tyrosinase, KRAS, p53, NRAS, HRAS, McPyV, CEA, CEACAM1, CEACAM6, CEACAM5, TREM2, CD71, alpha-synuclein, and / or an amyloid beta, or wherein the target comprises or is an MHC (e.g., HLA):antigen complex that comprises the antigen, or wherein the target comprises or is a label, such as FITC or a dinitrophenyl (DNP) such as 2,4-DNP, or a tag such as a Strep Tag (such as Strep-Tag or Strep-Tag II), a His Tag, a Myc Tag, a Flag Tag, or the like).

55. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, 43, and 46-54, the host cell of any one of claims 10, 11, and 14-54, the polynucleotide of any one of claims 12, 14-38, and 42-54, or the expression construct of any one of claims 13, 15-38, 42, 43, and 46-54, wherein the T cell or host cell encodes or express, or wherein the polynucleotide or expression construct encodes, two or more target-binding proteins, wherein the two or more target-binding proteins target different targets, wherein, optionally, the two or more target-binding proteins comprise: two or more CARs, two or more scTCRs, two or more multispecific T cell engagers, two or more TCRs, two or more IFPs, two or more synNotch receptors, two or more TCR / CARs, a CAR and a scTCR, a CAR and a multispecific T cell engager, a CAR and a TCR, a CAR and an IFP, a CAR and a synNotch receptor, a CAR and a TCR / CAR, a scTCR and a multispecific T cell engager, a multispecific T cell engager and an IFP, a multispecific T cell engager and a synNotch receptor, a TCR / CAR and a IFP, a TCR / CAR and a TCR, a TCR / CAR and a synNotch receptor, an IFP and a TCR, an IFP and a synNotch receptor, a scTCR and a TCR, a scTCR and an IFP, or a scTCR and a synNotch receptor.

56. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, 43, 45-54, the host cell of any one of claims 10, 11, and 14-54, the polynucleotide of any one of claims 12, 14-38, and 42- 54, or the expression construct of any one of claims 13, 15-38, 42, 43, and 45-54, wherein the Tcell or host cell encodes or expresses, or wherein the polynucleotide or expression construct encodes, two or more target-binding proteins, wherein the two or more target-binding proteins target different epitopes on the same target wherein, optionally, the two or more target-binding proteins comprise: two or more CARs, two or more scTCRs, two or more multispecific T cell engagers, two or more TCRs, two or more IFPs, two or more synNotch receptors, two or more TCR / CARs, a CAR and a scTCR, a CAR and a multispecific T cell engager, a CAR and a TCR, a CAR and an IFP, a CAR and a synNotch receptor, a CAR and a TCR / CAR, a scTCR and a multispecific T cell engager, a multispecific T cell engager and an IFP, a multispecific T cell engager and a synNotch receptor, a TCR / CAR and a IFP, a TCR / CAR and a TCR, a TCR / CAR and a synNotch receptor, an IFP and a TCR, an IFP and a synNotch receptor, a scTCR and a TCR, a scTCR and an IFP, or a scTCR and a synNotch receptor.

57. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, 43, 45-56, the host cell of any one of claims 10, 11, and 14-56, the polynucleotide of any one of claims 12, 14-38, and 42- 56, or the expression construct of any one of claims 13, 15-38, 42, 43, and 45-56, wherein the target-binding protein is multispecific and binds to, or wherein the T cell or host cell encodes or expresses, or wherein the polynucleotide or expression construct encodes, two or more (e.g., monospecific) target-binding proteins and the two or more target-binding proteins bind to different targets, wherein, optionally, the different targets comprise: CD19 and CD20, respectively; CD19 and CD22, respectively; GD2 and CD70, respectively; GD2 and CD56, respectively; GD2 and PSMA, respectively; CD70 and PSMA, respectively; BCMA and CD19, respectively; BCMA and TACI, respectively; CD19, CD20, and CD22, respectively; BCMA and GPRC5D, respectively; CD19 and CD70, respectively; CD19 and CD79b, respectively; CD20 and CD22, respectively; CD20 and CD79b, respectively; CD33 and CLL1, respectively; BCMA and SLAMF7, respectively; BCMA and CD229, respectively; GPRC5D and SLAMF7, respectively; GPRC5D and CD229, respectively; SLAMF7 and CD229, respectively; EphA2 and IL-13Rα2, respectively; HER2 and MUC1, respectively; EGFR, EpCAM, and HER2, respectively; HER2 and IL-13Rα2, respectively; GD2 and B7H3, respectively; CEA and MSLN, respectively; or CD19 and CD229, respectively.

58. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, 43, 46-57, the host cell of any one of claims 10, 11, and 14-57, the polynucleotide of any one of claims 12, 14-38, and42-57, or the expression construct of any one of claims 13, 15-38, 42, 43, and 46-57, wherein the target is an antigen expressed by cells of a hematological malignancy.

59. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, 43, 45-58, the host cell of any one of claims 10, 11, and 14-58, the polynucleotide of any one of claims 12, 14-38, and 42- 58, or the expression construct of any one of claims 13, 15-38, 42, 43, and 45-58, wherein the target is an antigen expressed by cells of a solid tumor.

60. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-59, the host cell of any one of claims 10, 11, and 14-59, the polynucleotide of any one of claims 12, 14-38, and 42-59, or the expression construct of any one of claims 13, 15-38, 42, 43, and 45-59, wherein the target-binding protein comprises an IFP, wherein, optionally, the target comprises: FasL, CD200, CD47, PVR aka CD155, TNF-α, a CSF (e.g., GM-CSF or G-CSF), PD-L1, PD-1, CD270 (HVEM), GAL9, CEACAM-1, phosphatidylserine (PtdSer), HMGB1, CTLA4, CD80, CD86, a B7-CD28 superfamily member, or combination of any two or more of the foregoing.

61. A vector comprising the polynucleotide of any one of claims 12, 14-38, and 42-60 or the expression construct of any one of claims 13, 15-38, 42, 43, and 45-60.

62. The vector of claim 61, which is a viral vector.

63. The vector of claim 62, which is a lentiviral vector.

64. The vector of claim 62, which is a retroviral vector, such as a γ-retroviral vector.

65. The vector of claim 62, which is an adeno-associated virus vector (AAV).

66. The vector of claim 62, which is derived from a baculovirus or an α-virus.

67. The vector of claim 61, which is a transposon vector.

68. The vector of claim 61, which is a Sleeping Beauty vector, a piggyBac vector, a mariner vector, a frog prince vector, a Tol2 vector, or a SPIN vector.

69. The vector of any one of claims 61-68, comprising the following features in 5’-- >3’ orientation: (i) [5’LTR]-[optional one, two, three, four, five, six, or more NFAT binding sites]-[ promoter 1]-[gene 1]-[promoter 2]-[gene 2]-[3’LTR], wherein: promoter 1 is optionally a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; and 3’LTR is optionally a self-inactivating LTR; or (ii) [5’LTR]-[one, two, three, four, five, six, or more NFAT binding sites]- [optional promoter 1]-[gene 1]-[promoter 2]-[gene 2]-[3’LTR], wherein: optional promoter 1 is a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; and 3’LTR is optionally a self-inactivating LTR.

70. The vector of any one of claims 61-68, comprising the following features in 3’-- >5’ orientation: (i) [3’ LTR]-[optional one to six NFAT binding sites]-[promoter 1]-[gene 1]- [polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]-[5’ LTR], wherein: promoter 1 is optionally a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; and 3’LTR is optionally a self-inactivating LTR; or (ii) [3’ LTR]-[one to six NFAT binding sites]-[optional promoter 1]-[gene 1]- [polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]-[5’ LTR], wherein: optional promoter 1 is a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; and 3’LTR is optionally a self-inactivating LTR.

71. The vector of claim 67, wherein the vector is a transposon vector, optionally a Sleeping Beauty vector or a piggyBac vector, and the vector comprises the following elements: (i) [3’ ITR]-[optional one to six NFAT binding sites]-[promoter 1]-[gene 1]- [polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]-[5’ ITR], wherein: each ITR is an inverted terminal repeat; promoter 1 is optionally a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target- binding protein and gene 2 encodes the fusion protein; (ii) [3’ ITR]-[one to six NFAT binding sites]-[optional promoter 1]-[gene 1]- [polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]-[5’ ITR], wherein: each ITR is an inverted terminal repeat; optional promoter 1 is a NFAT binding- inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; (iii) [3’ ITR]-[HS4 insulator]-[optional one to six NFAT binding sites]-[promoter 1]-[gene 1]-[polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]- [HS4 insulator]-[5’ ITR], wherein: each ITR is an inverted terminal repeat; promoter 1 is optionally a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target- binding protein and gene 2 encodes the fusion protein; (iv) [3’ ITR]-[HS4 insulator]-[one to six NFAT binding sites]-[optional promoter 1]-[gene 1]-[polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]- [HS4 insulator]-[5’ ITR], wherein: each ITR is an inverted terminal repeat; optional promoter 1 is a NFAT binding- inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; (v) [5’ ITR]-[optional one to six NFAT binding sites]-[promoter 1]-[gene 1]- [polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]-[3’ ITR], wherein: each ITR is an inverted terminal repeat; promoter 1 is optionally a NFAT binding-inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes thefusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target- binding protein and gene 2 encodes the fusion protein; (vi) [5’ ITR]-[one to six NFAT binding sites]-[optional promoter 1]-[gene 1]- [polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]-[3’ ITR], wherein each ITR is an inverted terminal repeat; optional promoter 1 is a NFAT binding- inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; (vii) [5’ ITR]-[HS4 insulator] [optional one to six NFAT binding sites]-[promoter 1]-[gene 1]-[polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]- [HS4 insulator]-[3’ ITR], wherein each ITR is an inverted terminal repeat; promoter 1 is optionally a NFAT- inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein; or (viii) [5’ ITR]-[HS4 insulator] [one to six NFAT binding sites]-[optional promoter 1]-[gene 1]-[polyadenylation signal 1]-[promoter 2]-[gene 2]-[polyadenylation signal 2]- [HS4 insulator]-[3’ ITR], wherein each ITR is an inverted terminal repeat; optional promoter 1 is a NFAT binding- inducible promoter; promoter 2 is optionally a constitutive promoter; gene 1 encodes the fusion protein and gene 2 encodes the target-binding protein, or gene 1 encodes the target-binding protein and gene 2 encodes the fusion protein.

72. A targeting polynucleotide construct comprising the polynucleotide of any one of claims 12, 14-38, and 42-60 or the expression construct of any one of claims 13, 15-38, 42, 43, and 45-60, and: a splice acceptor; and / or a sequence encoding a self-cleaving peptide or a cleavage site; and / or a left homology arm homologous to a first portion of a target locus; and / or a polyA sequence; and / or a right homology arm homologous to a second portion of a target locus,wherein, optionally, the target locus comprises safe harbor locus, wherein, further optionally, the target locus is or comprises a (e.g., human) TRAC, TRBC, Rosa26, AAVS1, CCR5, CD8α, CD8β, CD4 (see, e.g., Xu et al., Cell Stem Cell 24(4):P566-587.E7 (2019), doi.org / 10.1016 / j.stem.2019.02.005), PDCD1 (PD1), TIGIT, LAG3, BTLA, CTLA4, HAVCR3 (TIM3), TNFRSF18 (GITR), CD47 (see, e.g., Yamada-Hunter et al., Nature (2024), doi.org / 10.1038 / s41586-024-07443-8), HLA-A, HLA-B, HLA-C, B2M, or CD40L locus.

73. A kit or system comprising: the targeting polynucleotide construct of claim 72; a guide RNA targeting a portion of the target locus; and a polynucleotide (e.g., mRNA) or vector (e.g., a viral vector) encoding a Cas protein (e.g., Cas9), or a Cas protein and optional amphilphilic peptides for delivery of the Cas protein (see, e.g., Voss et al., Nat Biomed Eng.2023 May;7(5):647-660. doi: 10.1038 / s41551-023-01032-2).

74. A host cell comprising the polynucleotide of any one of claims 12, 14-38, and 42- 60, the expression construct of any one of claims 13, 15-38, 42, 43, and 46-60, the vector of any one of claims 61-71, or the targeting polynucleotide construct of claim 72, wherein, optionally, the host cell comprises a human cell, an immune system cell, a hematopoietic progenitor cell, a stem cell, a peripheral blood mononuclear cell (PBMC), or any combination thereof, wherein, further optionally, the host cell comprises a T cell, a NK cell, a NK-T cell, a dendritic cell, a macrophage, a B cell, a monocyte, or any combination thereof, wherein, even further optionally, the host cell comprises a CD4+ T cell, a CD8+ T cell, a CD4- CD8- double negative T cell, a γδ T cell, a naïve T cell, a central memory T cell, a stem cell memory T cell, an effector memory T cell, a tumor infiltrating lymphocyte (TIL), or any combination thereof.

75. A cell population or composition comprising a plurality of the T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-60 and / or a plurality of the host cell of any one of claims 10, 11, 14-59, and 74.

76. A composition comprising: (1) the T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-60; the host cell of any one of claims 10, 11, 14-59, and 74; the polynucleotide of any one of claims 12, 14- 38, and 42-60; the expression construct of any one of claims 13, 15-38, 42, 43, and 46-60; thevector of any one of claims 61-71; the targeting polynucleotide construct of claim 72; and / or the cell population or composition of claim 75; and (2) a pharmaceutically acceptable carrier, excipient, or diluent, wherein, optionally: the composition comprises CD8+ T cells encoding or expressing the fusion protein and an antigen-specific MHC Class I-restricted TCR, and the composition further comprises CD4+ T cells encoding or expressing the antigen-specific MHC Class I-restricted TCR and a CD8αβ co- receptor polypeptide; and / or the composition comprises CD8+ T cells encoding or expressing the fusion protein and an antigen-specific CAR, and the composition further comprises CD4+ T cells encoding or expressing the antigen-specific CAR; and / or the composition comprises tumor infiltrating lymphocytes (TILs); and / or the composition further comprises a checkpoint inhibitor antibody or antigen-binding fragment thereof, wherein the checkpoint inhibitor antibody or antigen-binding fragment thereof optionally comprises an anti-PD1 antibody or antigen-binding fragment thereof, an anti-PD-L1 antibody or antigen-binding fragment thereof, an anti-CTLA4 antibody or antigen-binding fragment thereof, an anti-LAG3 antibody or antigen-binding fragment thereof, an anti-TIM3 antibody or antigen-binding fragment thereof, an anti-TIGIT antibody or antigen-binding fragment thereof, an anti-GITR antibody or antigen-binding fragment thereof, an anti-CD40 antibody or antigen-binding fragment thereof, an anti-CD137 antibody or antigen-binding fragment thereof, an anti-VISTA antibody or antigen-binding fragment thereof, an anti-CD47 antibody or antigen-binding fragment thereof, an anti-KIR antibody or antigen-binding fragment thereof, an anti-ICOS antibody or antigen-binding fragment thereof, an anti-CD20 antibody or antigen-binding fragment thereof, an anti-CD155 antibody or antigen-binding fragment thereof, an anti-PVRIG antibody or antigen-binding fragment thereof, an anti-B7-H4 antibody or antigen- binding fragment thereof, an anti-B7-H3 antibody or antigen-binding fragment thereof, an anti- CD244 / 2B4 antibody or antigen-binding fragment thereof, an anti-HVEM antibody or antigen- binding fragment thereof, an anti-BTLA antibody or antigen-binding fragment thereof, an anti- CD160 antibody or antigen-binding fragment thereof, an anti-GAL9 antibody or antigen-binding fragment thereof, an anti-PVRL3 antibody or antigen-binding fragment thereof, an anti-LAIR1 antibody or antigen-binding fragment thereof, an antibody or antigen-binding fragment that targets an immunosuppressive cytokine such as IL-10, IL-4, IL-1RA, or IL-35), an anti-IDOantibody or antigen-binding fragment thereof, an anti-CEACAM-1 antibody or antigen-binding fragment thereof, an anti-CEACAM-3 antibody or antigen-binding fragment thereof, an anti- CEACAM-5 antibody or antigen-binding fragment thereof, an antibody or antigen-binding fragment that targets Treg cells, an anti-adenosine antibody or antigen-binding fragment thereof, an anti-A2aR antibody or antigen-binding fragment thereof, or any combination of two or more of the foregoing.

77. The composition of claim 76, wherein the polynucleotide, expression construct, or targeting polynucleotide construct is comprised in a carrier, wherein the carrier comprises a lipid, a lipid-derived delivery vehicle, such as a liposome, a solid lipid nanoparticle, an oily suspension, a submicron lipid emulsion, a lipid microbubble, an inverse lipid micelle, a cochlear liposome, a lipid microtubule, a lipid microcylinder, lipid nanoparticle (LNP), a lipopolyplex (LPP), a cationic polypeptide, a polymeric nanoparticle, or a nanoscale platform, such as a nanoemulsion.

78. A method comprising introducing into a host cell: the polynucleotide of any one of claims 12, 14-38, and 42-60; the expression construct of any one of claims 13, 15-38, 42, 43, and 46-60; the vector of any one of claims 61-71; the targeting polynucleotide construct of claim 72, or the composition of claim 76 or 77, wherein, optionally, (1) the host cell comprises a human cell, an immune system cell, a hematopoietic progenitor cell, a stem cell, a peripheral blood mononuclear cell (PBMC), or any combination thereof, wherein, further optionally, the host cell comprises a T cell, a NK cell, a NK-T cell, a dendritic cell, a macrophage, a monocyte, or any combination thereof, wherein, even further optionally, the host cell comprises a CD4+ T cell, a CD8+ T cell, a CD4- CD8- double negative T cell, a γδ T cell, a naïve T cell, a central memory T cell, a stem cell memory T cell, an effector memory T cell, a tumor infiltrating lymphocyte (TIL), or any combination thereof, and / or (2) the method is performed in vitro, in vivo, or ex vivo.

79. A host cell made by the method of claim 78.

80. A method for treating a disease or disorder in a subject, the method comprising administering to the subject an effective amount of: the T cell of any one of claims 1, 3, 4, 5, 11,14-38, 42, 43, and 45-60; the host cell of any one of claims 10, 11, 14-60, 74, and 79; the polynucleotide of any one of claims 12, 14-38, and 42-60; the expression construct of any one of claims 13, 15-38, 42, 43, and 46-60; the vector of any one of claims 61-71; the targeting polynucleotide construct of claim 72; the composition of claim 76 or 77; and / or the cell population of claim 75, wherein, optionally: the method comprises administering to the subject an effective amount of CD8+ T cells encoding or expressing the fusion protein and an antigen-specific MHC Class I-restricted TCR, and further administering to the subject an effective amount of CD4+ T cells encoding or expressing the antigen-specific MHC Class I-restricted TCR and a CD8αβ co-receptor polypeptide; and / or the method comprises administering to the subject an effective amount of CD8+ T cells encoding or expressing the fusion protein and an antigen-specific CAR, and further administering to the subject an effective amount of CD4+ T cells encoding or expressing the antigen-specific CAR; and / or the method further comprises administering to the subject an effective amount of a checkpoint inhibitor antibody or antigen-binding fragment thereof, wherein the checkpoint inhibitor antibody or antigen-binding fragment thereof optionally comprises an anti-PD1 antibody or antigen-binding fragment thereof (e.g., Opdivo® 240 mg every 2 weeks or 480 mg every 4 weeks), an anti-PD-L1 antibody or antigen-binding fragment thereof, an anti-CTLA4 antibody or antigen-binding fragment thereof, , an anti-LAG3 antibody or antigen-binding fragment thereof, an anti-TIM3 antibody or antigen-binding fragment thereof, an anti-TIGIT antibody or antigen-binding fragment thereof, an anti-GITR antibody or antigen-binding fragment thereof, an anti-CD40 antibody or antigen-binding fragment thereof, an anti-CD137 antibody or antigen-binding fragment thereof, an anti-VISTA antibody or antigen-binding fragment thereof, an anti-CD47 antibody or antigen-binding fragment thereof, an anti-KIR antibody or antigen-binding fragment thereof, an anti-ICOS antibody or antigen-binding fragment thereof, an anti-CD20 antibody or antigen-binding fragment thereof, an anti-CD155 antibody or antigen-binding fragment thereof, an anti-PVRIG antibody or antigen-binding fragment thereof, an anti-B7-H4 antibody or antigen-binding fragment thereof, an anti-B7-H3 antibody or antigen-binding fragment thereof, an anti-CD244 / 2B4 antibody or antigen-binding fragment thereof, an anti-HVEM antibody or antigen-binding fragment thereof, an anti-BTLAantibody or antigen-binding fragment thereof, an anti-CD160 antibody or antigen-binding fragment thereof, an anti-GAL9 antibody or antigen-binding fragment thereof, an anti-PVRL3 antibody or antigen-binding fragment thereof, an anti-LAIR1 antibody or antigen-binding fragment thereof, an antibody or antigen-binding fragment that targets an immunosuppressive cytokine such as IL-10, IL-4, IL-1RA, or IL-35), an anti-IDO antibody or antigen-binding fragment thereof, an anti-CEACAM-1 antibody or antigen-binding fragment thereof, an anti- CEACAM-3 antibody or antigen-binding fragment thereof, an anti-CEACAM-5 antibody or antigen-binding fragment thereof, an antibody or antigen-binding fragment that targets Treg cells, an anti-adenosine antibody or antigen-binding fragment thereof, an anti-A2aR antibody or antigen-binding fragment thereof, or any combination of two or more of the foregoing.

81. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-60, the host cell of any one of claims 10, 11, 14-60, 74, and 79, the polynucleotide of any one of claims 12, 14-38, and 42-60, the expression construct of any one of claims 13, 15-38, 42, 43, and 46-60, the vector of any one of claims 61-71, the targeting polynucleotide construct of claim 72, the composition of claim 76 or 77, and / or the cell population of claim 75, for use in a method of treating a disease or disorder in a subject.

82. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-60, the host cell of any one of claims 10, 11, 14-60, 74, and 79, the polynucleotide of any one of claims 12, 14-38, and 42-60, the expression construct of any one of claims 13, 15-38, 42, 43, and 46-60, the vector of any one of claims 61-71, the targeting polynucleotide construct of claim 72; the composition of claim 76 or 77, and / or the cell population of claim 75, for use in the manufacture of a medicament for treating a disease or disorder in a subject.

83. The T cell of any one of claims 1, 3, 4, 5, 11, 14-38, 42, 43, and 45-60, the host cell of any one of claims 10, 11, 14-60, 74, and 79, the polynucleotide of any one of claims 12, 14-38, and 42-60, the expression construct of any one of claims 13, 15-38, 42, 43, and 46-60, the vector of any one of claims 61-71, the targeting polynucleotide construct of claim 72; the composition of claim 76 or 77, and / or the cell population of claim 75, for use as a medicament.

84. The method of claim 80 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of any one of claims 81-83, wherein the disease or disorder is selected from a hyperproliferative disease or disorder, a proliferative disease or disorder, an autoimmune disease or disorder, a neurodegenerative disease or disorder, a neurological disease or disorder, an aging-related disease or disorder, a bacterial infection, a viral infection, a fungal infection, and a parasitic infection.

85. The method of claim 84 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of claim 84, wherein the disease or disorder comprises a cancer.

86. The method of claim 85 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of claim 85, wherein the cancer is a hematologic malignancy.

87. The method of claim 85 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of claim 85, wherein the cancer is a solid cancer.

88. The method of claim 85 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of claim 85, wherein the cancer is selected from a carcinoma, a melanoma, a sarcoma, a glioma, a lymphoma, a leukemia, and a myeloma.

89. The method of claim 85 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of claim 85, wherein the cancer comprises: a cancer of the head or neck, melanoma, pancreatic cancer, cholangiocarcinoma, hepatocellular cancer, breast cancer including triple-negative breast cancer (TNBC), gastric cancer, non-small-cell lung cancer, prostate cancer (e.g., castration- resistant prostate cancer or castration-resistant metastatic prostate cancer), esophageal cancer, mesothelioma, small-cell lung cancer, colorectal cancer, glioblastoma, Askin's tumor, sarcomabotryoides, chondrosarcoma, Ewing's sarcoma, PNET, malignant hemangioendothelioma, malignant schwannoma, osteosarcoma, alveolar soft part sarcoma, angiosarcoma, cystosarcoma phyllodes, dermatofibrosarcoma protuberans (DFSP), desmoid tumor, desmoplastic small round cell tumor, epithelioid sarcoma, extraskeletal chondrosarcoma, extraskeletal osteosarcoma, fibrosarcoma, gastrointestinal stromal tumor (GIST), hemangiopericytoma, hemangiosarcoma, Kaposi's sarcoma, leiomyosarcoma, liposarcoma, lymphangiosarcoma, lymphosarcoma, undifferentiated pleomorphic sarcoma, malignant peripheral nerve sheath tumor (MPNST), neurofibrosarcoma, rhabdomyosarcoma, synovial sarcoma, undifferentiated pleomorphic sarcoma, squamous cell carcinoma, basal cell carcinoma, adenocarcinoma, linitis plastic, vipoma, cholangiocarcinoma, hepatocellular carcinoma, adenoid cystic carcinoma, renal cell carcinoma, Grawitz tumor, ependymoma, astrocytoma, oligodendroglioma, brainstem glioma, optice nerve glioma, a mixed glioma, Hodgkin’s lymphoma, a B-cell lymphoma, non-Hodgkin’s lymphoma (NHL), Burkitt's lymphoma, acute lymphoblastic leukemia (ALL) small lymphocytic lymphoma (SLL), diffuse large B-cell lymphoma, follicular lymphoma (CL), immunoblastic large cell lymphoma, precursor B-lymphoblastic lymphoma, mantle cell lymphoma, Waldenström's macroglobulinemia, CD37+ dendritic cell lymphoma, lymphoplasmacytic lymphoma, splenic marginal zone lymphoma, extra-nodal marginal zone B cell lymphoma of mucosa-associated (MALT) lymphoid tissue, nodal marginal zone B-cell lymphoma, mediastinal (thymic) large B-cell lymphoma, intravascular large B-cell lymphoma, primary effusion lymphoma, adult T-cell lymphoma, extranodal NK / T-cell lymphoma, nasal type, enteropathy- associated T-cell lymphoma, hepatosplenic T-cell lymphoma, blastic NK cell lymphoma, Sezary syndrome, angioimmunoblastic T cell lymphoma, anaplastic large cell lymphoma, chronic lymphocytic leukemia (CLL), chronic myeloid leukemia, chondrosarcoma, fibrosarcoma (fibroblastic sarcoma), Dermatofibrosarcoma protuberans (DFSP), osteosarcoma, rhabdomyosarcoma, Ewing’s sarcoma, a gastrointestinal stromal tumor, Leiomyosarcoma, angiosarcoma (vascular sarcoma), Kaposi’s sarcoma, liposarcoma, pleomorphic sarcoma, synovial sarcoma, a lung carcinoma (e.g., Adenocarcinoma, Squamous Cell Carcinoma (Epidermoid Carcinoma), Squamous cell carcinoma, Adenocarcinoma, Adenosquamous carcinoma, anaplastic carcinoma; Large cell carcinoma, Small cell carcinoma, a breast carcinoma (e.g., Ductal Carcinoma in situ (non-invasive), Lobular carcinoma in situ (non-invasive), Invasive Ductal Carcinoma, Invasive lobular carcinoma, Non-invasive Carcinoma), a liver carcinoma (e.g., Hepatocellular Carcinoma, Cholangiocarcinomas or Bile Duct Cancer), Large-cell undifferentiated carcinoma, Bronchioalveolar carcinoma), an ovarian carcinoma (e.g., Surface epithelial-stromal tumor (Adenocarcinoma) or ovarian epithelial carcinoma (which includes serous tumor, endometrioid tumor and mucinous cystadenocarcinoma), Epidermoid (Squamous cell carcinoma), Embryonal carcinoma and choriocarcinoma (germ cell tumors)), a kidney carcinoma (e.g., Renal adenocarcinoma, hypernephroma, Transitional cell carcinoma (renal pelvis), Squamous cell carcinoma, Bellini duct carcinoma, Clear cell adenocarcinoma, Transitional cell carcinoma, Carcinoid tumor of the renal pelvis), an adrenal carcinoma (e.g., Adrenocortical carcinoma), a carcinoma of the testis (e.g., Germ cell carcinoma (Seminoma, Choriocarcinoma, Embryonal carciroma, Teratocarcinoma), Serous carcinoma), Gastric carcinoma (e.g., Adenocarcinoma), an intestinal carcinoma (e.g., Adenocarcinoma of the duodenum), a colorectal carcinoma, a skin carcinoma (e.g., Basal cell carcinoma, Squamous cell carcinoma), an ovarian carcinoma, an ovarian epithelial carcinoma, a cervical adenocarcinoma or small cell carcinoma, a pancreatic carcinoma, a colorectal carcinoma (e.g., an adenocarcinoma or squamous cell carcinoma), a lung carcinoma, a breast ductal carcinoma, Merkel Cell Carcinoma, and / or an adenocarcinoma of the prostate.

90. The method of any one of claims 80 and 84-89 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of claim 84-89, wherein the subject is human.

91. The method of any one of claims 80 and 84-89 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of claim 84-89, wherein the subject has not received or does not receive chemotherapy pre-conditioning (e.g., comprising fludarabine, cyclophosphamide, pentostatin, bendustamine, oxaliplatin, or any combination thereof).

92. The method of any one of claims 79, 80, and 84-91 or the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population for use of claim 84-91, wherein the cell is autologous to the subject, is allogeneic to the subject, or is produced in the subject.

93. A kit comprising:(i) the T cell of any one of claims 1, 11, 14-38, 42, 43, and 45-60; the host cell of any one of claims 10, 11, 14-60, 74, and 79; the polynucleotide of any one of claims 12, 14-38, and 42-60; the expression construct of any one of claims 13, 15-38, 42, 43, and 46-60; the vector of any one of claims 61-71; the targeting polynucleotide construct of claim 72; the composition of claim 76 or 77; and / or the cell population of claim 75; and any one or more of (ii)-(iv): (ii) a container for the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population; (iii) a means for delivering the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population into a subject (e.g., an intravenous delivery system, a syringe, or the like); (iv) instructions for delivering the polynucleotide, expression construct, vector, or targeting polynucleotide construct into a host cell, or for delivering the T cell, host cell, polynucleotide, expression construct, vector, targeting polynucleotide construct, composition, or cell population into a subject.

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