{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRetinoic acid receptor gamma (RARγ) is emerging as a versatile regulator of cell fate. Enhanced retinoic acid signaling through RARγ, particularly when combined with factors such as liver receptor homolog‐1, accelerates the reprogramming of somatic cells to induced pluripotent stem cells and facilitates the establishment of a ground‐state, naïve pluripotency."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " In addition, activation of RARγ is indispensable for osteogenic transdifferentiation in myoblasts and for promoting differentiation in leukemic cells exposed to selective retinoids."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPathogenic variants in RARγ have been implicated in adverse drug reactions. In models of doxorubicin-induced cardiotoxicity, a missense mutation in RARG (p.Ser427Leu) disrupts normal transcriptional repression of targets such as Top2β, thereby increasing sensitivity to cardiotoxic stress in both patient cohorts and induced pluripotent stem cell–derived cardiomyocytes."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": " Moreover, RARγ activation is essential for triggering apoptosis in pancreatic adenocarcinoma cells, underscoring its potential relevance in cancer therapy."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the hematopoietic compartment, fusion proteins involving RARγ – for example, NUP98–RARG – confer transforming activity on progenitor cells and endow them with heightened sensitivity to retinoid-induced differentiation, thereby contributing to leukemogenesis and influencing cell cycle regulators such as CDK1."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": " Beyond malignant transformation, genetic variations in RARγ are associated with altered cytokine responses following rubella vaccination, and downregulation of RARγ in tumor-associated macrophages correlates with enhanced inflammatory signaling within the tumor microenvironment."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn hormone-responsive tissues, RARγ modulates cross-talk with other nuclear receptors. In the prostate, RARγ contributes to the regulation of genes such as hTGP in cooperation with the androgen receptor, and its altered expression correlates with tumor progression."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": " In cholangiocarcinoma and hepatocellular carcinoma, aberrant overexpression of RARγ drives oncogenic signaling through pathways including Wnt/β-catenin, Akt/NF-κB and suppression of p53, whereas in colorectal cancer it may exert tumor-suppressive effects by engaging Hippo-Yap signaling. Additionally, RARγ-dependent cross-talk with progesterone receptor pathways influences the expansion of therapy-resistant cell subpopulations in breast cancer."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRARγ is distinguished from other retinoic acid receptor isotypes by its unique transcriptional properties. It displays limited binding to corepressor proteins (e.g. SMRT), enabling significant hormone-independent transcriptional activation—a property linked to specific features within its helix 3 region."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": " Its activity is further fine-tuned through interactions with cofactors such as vinexin beta, which bind to the receptor’s AF-1 domain in a phosphorylation-sensitive manner."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": " Moreover, the dynamic subcellular localization of RARγ—regulated by ligand binding, receptor heterodimerization with RXR, and proteasome-mediated degradation—further modulates its transcriptional output."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "22"}]}, {"type": "t", "text": " RARγ also interfaces with other nuclear receptor pathways, as demonstrated by its ability to interact with vitamin D response elements and modify vitamin D receptor signaling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional extranuclear functions of RARγ have been identified. Under stress conditions, cytoplasmic RARγ facilitates the assembly of RIP1-dependent death signaling complexes that mediate apoptosis and necroptosis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "25"}]}, {"type": "t", "text": " Furthermore, a reduction in RARγ mRNA expression in peripheral blood mononuclear cells and subcutaneous adipose tissue of obese subjects suggests its broader involvement in metabolic regulation and systemic retinoid signaling homeostasis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Wei Wang, Jian Yang, Hui Liu, et al. 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