{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTRIM25 is a pivotal E3 ubiquitin ligase that initiates antiviral defense by catalyzing Lys63‐linked polyubiquitination of the caspase activation and recruitment domains (CARDs) of the RIG‑I viral RNA sensor, thereby promoting its association with downstream adaptors and triggering type I interferon production. In this capacity, TRIM25 functions at a critical early step in host innate immunity, a process that is frequently subverted by viral antagonists—such as the influenza A virus NS1 protein, dengue virus subgenomic flavivirus RNA, SARS‑CoV nucleocapsid, RSV NS1, and paramyxovirus V proteins—which bind to specific regions (often the coiled‐coil or SPRY domain) of TRIM25, block its multimerization or proper positioning, and ultimately suppress RIG‑I CARD ubiquitination and downstream interferon signaling. In addition, cellular factors—including deubiquitinases and competing ubiquitin ligase complexes (e.g. LUBAC)—further modulate TRIM25’s stability and activity to fine‐tune the antiviral response."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its central role in antiviral signaling, TRIM25 functions as an RNA‐binding protein that modulates a broad spectrum of cellular processes. It has been implicated as an RNA cofactor in Lin28a/TuT4‐mediated pre‑let‑7 uridylation and in regulating the stability and translation of mRNAs. TRIM25 also exerts profound effects on cell proliferation, differentiation, and tumorigenesis by governing the turnover or activity of key regulatory proteins—including p53, ERG, and peroxisome proliferator‑activated receptor γ (PPARγ)—and by promoting NF‑κB signaling through K63‑linked ubiquitination of TRAF2. Furthermore, TRIM25 contributes to cellular homeostasis by maintaining endoplasmic reticulum redox balance through degradation of Keap1 and subsequent activation of Nrf2, while its activity is itself tightly controlled by interactions with deubiquitinases (such as USP15, OTUD5, and USP10) and by post‑translational modifications that impact its dimerization and substrate specificity. Dysregulation of TRIM25 has been associated with enhanced oncogenic signaling in lung, prostate, and breast cancers, as well as with altered differentiation processes in hematopoietic cells."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "36"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Michaela U Gack, Axel Kirchhofer, Young C Shin, et al. 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