{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nUCHL5 (also known as Uch37) is a deubiquitinating enzyme that is intricately regulated by its association with the 26S proteasome. It is recruited to the proteasome via binding to the ubiquitin receptor hRpn13/Adrm1, an interaction that not only positions UCHL5 close to its ubiquitinated substrates but also relieves its intrinsic autoinhibition. In complex with the proteasome, UCHL5 selectively removes ubiquitin moieties—such as trimming distal Lys48‐linked chains and debranching complex polyubiquitin architectures—to facilitate substrate processing and efficient protein degradation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical proteolytic role, UCHL5 modulates key signaling pathways by directly regulating the ubiquitination status of pivotal regulatory proteins. It deubiquitinates components of the transforming growth factor–β (TGF‑β) cascade—stabilizing Smad2/3—as well as transcription factors such as E2F1, thereby enhancing their transcriptional activity. In addition, UCHL5 influences Wnt/β‑catenin and Tcf/Lef signaling, as evidenced by its role in promoting the chromatin occupancy of Tcf7. Collectively, these actions underscore a role for UCHL5 as an important regulator of cellular signaling and gene expression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDeregulation of UCHL5 has been implicated in the pathogenesis and progression of several cancers. Increased expression and/or hyperactivity of UCHL5 is observed in multiple myeloma, hepatocellular carcinoma, esophageal squamous cell carcinoma, ovarian cancer, Waldenström macroglobulinemia, pancreatic adenocarcinoma, colorectal cancer, and gastric cancer. Its aberrant activity is linked to enhanced proliferation, impaired degradation of oncogenic substrates, and resistance to conventional proteasome inhibitors. Moreover, pharmacological inhibition of UCHL5 (often in combination with inhibition of the homologous protease USP14) has demonstrated promising antitumor activity by instigating growth arrest, apoptosis, and cell‐cycle perturbations."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its roles at the proteasome and in signal transduction, UCHL5 contributes to other critical cellular processes. It functions as a component of the INO80 chromatin‐remodeling complex, thereby influencing transcription and DNA repair, and structural analyses have revealed that UCHL5 can adopt distinct conformations that dictate its catalytic potential. 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