{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nUSP39 is increasingly recognized as an essential regulator of pre‐mRNA processing. Although it harbors a ubiquitin‐protease domain, USP39 lacks classical deubiquitinating activity in several contexts and instead functions as a pivotal component of the spliceosome. It facilitates the splicing and maturation of key mRNAs—including those encoding Aurora B, and factors essential for proper mitotic checkpoint function and B cell development—thus ensuring precise chromosome segregation and immunoglobulin gene rearrangement. These findings underscore its fundamental role in RNA maturation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its splicing functions, USP39 is frequently overexpressed in a wide range of cancers—including breast, hepatocellular, prostate, colorectal, ovarian, pancreatic, lung, gastric, melanoma, nasopharyngeal, glioma, and leukemia—where its dysregulation is closely correlated with increased cell proliferation, colony formation, migration, invasion, and resistance to apoptosis. Experimental knockdown studies in diverse tumor models have demonstrated that USP39 loss leads to cell cycle arrest (often at G2/M), impaired mRNA maturation of critical cell‐cycle regulators (e.g. FoxM1, cyclin B1, TAZ), and enhanced chemosensitivity. 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