{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nUSP25 is a deubiquitinating enzyme that plays a critical role in post‐translational protein regulation. Early studies identified USP25 as a unique ubiquitin‐specific protease with tissue‐selective expression and structural features including ubiquitin‐binding domains and motifs that bind the SUMO modifiers. In particular, its UIMs and a SUMO interaction motif confer both the capacity to bind SUMO2/3 and to undergo sumoylation, which in turn impairs its binding to and hydrolysis of ubiquitin chains. In silico and structural analyses of isoforms, including the muscle variant, further reveal that USP25’s catalytic activity is modulated by intramolecular interactions and auto‐regulatory loops. This complexity, as reviewed among deubiquitinating enzymes, underscores the importance of post‐translational modifications in dictating USP25 function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its autoregulatory control, USP25 influences multiple cellular signaling pathways by modifying the ubiquitination status of key substrates. It counteracts ubiquitination in endoplasmic reticulum–associated degradation and modulates innate immune responses by deubiquitinating mediators such as RIG-I and TRAF2/6, thereby suppressing virus‐induced type I interferon production. USP25 also promotes Wnt/β‐catenin signaling by directly interacting with and deubiquitinating tankyrases—leading to tankyrase stabilization and down‐regulation of the scaffold protein Axin—as well as stabilizing oncoproteins like BCR‐ABL. Recent structural work has further revealed that USP25 can adopt distinct oligomeric states (including dimeric and autoinhibited tetrameric assemblies) that directly affect its catalytic activity, a feature exploited in the development of specific inhibitors."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "18"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its biochemical functions, altered USP25 activity or expression is emerging as an important contributor to diverse human diseases. For example, downregulation or deletion of USP25 has been linked to loss‐of-heterozygosity events in lung cancer, while genetic and functional studies implicate USP25 variants in neurological disorders including epilepsy and the neurodevelopmental abnormalities associated with Down syndrome. Aberrant USP25 expression also influences inflammatory bowel conditions, allergic rhinitis, and tissue remodeling events such as trophoblast epithelial-to-mesenchymal transition in recurrent miscarriage. Furthermore, USP25 has been associated with gastrointestinal infections and tumorigenesis, hepatocellular carcinoma, pancreatitis, and even aspects of EGFR recycling and signal modulation. In these contexts, USP25 not only acts as a regulator of protein stability and immune signaling but also represents a promising therapeutic target whose modulation might ameliorate cancer, inflammatory, and neurodevelopmental diseases."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "31"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "R Valero, M Bayés, M Francisca Sánchez-Font, et al. 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