泛素特异性蛋白酶5的生物学作用及其在肿瘤中的研究进展OA

Ubiquitin-specific protease 5(USP5),also known as isopeptidase T(IsoT),functions as a key member of the deubiquitinating enzyme family.It regulates target protein stability by hydrolyzing unanchored polyubiquitin chains and plays multiple oncogenic roles in tumorigenesis and progression.This article elaborates on the structure and biological functions of USP5.USP5 is a multi-domain enzyme composed of 835 amino acid residues,featuring a zinc finger ubiquitin-specific protease domain(ZnF-UBP),a UBP domain,and two ubiquitin-associated domains.It plays crucial biological roles in maintaining protein stability,participating in tumor-related signaling pathways,exerting extracellular biological effects,and regulating tumor cell cycle,apoptosis,and metabolic reprogramming.In terms of advances in tumor research,USP5 has demonstrated significant potential as a diagnostic marker,therapeutic target,and prognostic biomarker in various cancers.Although certain achievements have been made in cancer therapy through related inhibitors and strategies that regulate USP5 expression or activity,further studies are still needed to overcome existing limitations.Future comprehensive clinical investigations and in-depth analysis and integration of molecular mechanisms will provide new perspectives and directions for tumor diagnosis,treatment,and prognosis evaluation.