泛素
泛素结合酶
生物
蛋白酶体
脱氮酶
酶
细胞生物学
癌症
癌症研究
生物化学
遗传学
泛素连接酶
基因
作者
Keshen Wang,Qichen He,Xiangyan Jiang,Yong Ma,Tao Wang,Huinian Zhou,Zeyuan Yu,Zuoyi Jiao
标识
DOI:10.2174/0115680096370867250211070948
摘要
The ubiquitin-proteasome system is a fundamental regulatory mechanism that governs protein stability and intracellular signaling in eukaryotic cells. This system relies on a coordinated cascade of enzymatic activities involving activating enzymes, conjugating enzymes, and ligases to assemble distinct ubiquitin signals. These signals are subsequently edited, removed, or interpreted by deubiquitinases and ubiquitin-binding proteins. While E3 ligases have traditionally been recognized as the primary determinants of substrate specificity in the ubiquitination process, recent studies have revealed that the dysregulation of E2 enzymes can also lead to significant pathological outcomes, including chromatin instability, immune dysregulation, metabolic dysfunction, and an elevated risk of cancer. Consequently, E2 enzymes have emerged as promising therapeutic targets for the treatment of various dis-eases. This review provides a comprehensive examination of the roles and mechanisms of the ubiquitin-conjugating enzyme E2T (UBE2T) in cancer initiation, progression, and therapy resistance, highlighting its potential as a compelling target for cancer therapeutics.
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