{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTRIM33 (also known as TIF1γ) is a pivotal modulator of transforming growth factor‐β (TGFβ) signaling and transcriptional regulation. It functions by binding receptor‐activated Smad2/3 complexes in lieu of Smad4, thereby generating an alternative branch of TGFβ responses that govern cell fate decisions. In diverse cellular contexts—including embryonic stem cells, hematopoietic progenitors and mammary epithelia—TRIM33’s specialized PHD–bromodomain reads specific chromatin marks (e.g. H3K9me3 and H3K18ac) to render previously “poised” developmental regulators accessible for transcription. In addition, TRIM33 modulates transcription elongation and post‐translational modifications such as Smad4 ubiquitination and SnoN sumoylation, all of which fine‐tune the intensity and duration of TGFβ signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of cancer, TRIM33 exhibits multifaceted roles that are both tumor‐suppressive and, under certain conditions, oncogenic. Loss or down‐regulation of TRIM33 has been linked to pancreatic tumorigenesis, chronic myelomonocytic leukemia and hepatocellular carcinoma, while in other scenarios its activity—via degradation of nuclear β‐catenin or by modulating epithelial–mesenchymal transition (EMT) through Smad complex regulation—limits tumor cell invasion and chromosomal instability. Moreover, aberrant TRIM33 expression and autoantibodies against it serve as biomarkers in cancer‐associated dermatomyositis and related malignancies; altered expression in clear cell renal carcinoma and modulation by microRNAs further underscore its impact on cancer progression. Notably, TRIM33 is also subject to regulation by upstream factors (for example, repression by SOX2 or phosphorylation by c‐Abl) that influence its capacity to restrain TGFβ‐mediated EMT in non–small‐cell lung cancer and other tumors, and its gene is being deeply sequenced in cancer‐associated myositis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in cell fate and tumor suppression, TRIM33 is instrumental in immune regulation and antiviral defense. It participates in innate immune responses by promoting the activation of the NLRP3 inflammasome through ubiquitination of the RNA sensor DHX33 and by restricting viral replication—for example, by targeting HIV‐1 integrase for degradation. TRIM33 is also co‐opted by viral proteins such as adenovirus E4‐ORF3, which relocalizes or induces its sumoylation, thereby modulating the cellular environment during infection. In addition, emerging studies have implicated TRIM33 in regulating inflammatory conditions such as colitis, idiopathic pulmonary fibrosis and psoriasis, as well as in retroviral silencing in embryonic stem cells and even neurodevelopmental disorders including autism."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "32", "end_ref": "42"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn additional physiological contexts, TRIM33 contributes to the maintenance of tissue integrity. For example, in osteoblasts it protects against oxidative stress–induced apoptosis by restraining FOXO3a ubiquitination, thus implicating TRIM33 in bone homeostasis and the pathogenesis of osteoporosis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "43"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Hongzhuang Peng, Irina Feldman, Frank J Rauscher "}, {"type": "b", "children": [{"type": "t", "text": "Hetero-oligomerization among the TIF family of RBCC/TRIM domain-containing nuclear cofactors: a potential mechanism for regulating the switch between coactivation and corepression."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Biol (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/S0022-2836(02)00477-1"}], "href": "https://doi.org/10.1016/S0022-2836(02"}, {"type": "t", "text": "00477-1) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12096914"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12096914"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Wei He, David C Dorn, Hediye Erdjument-Bromage, et al. 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