非经典泛素化的研究进展  

Advances of nonclassical ubiquitination

作　　者：杨昱鸽 张文阳 李振斐 盛相鹏 胡荣贵 YANG Yuge;ZHANG Wenyang;LI Zhenfei;SHENG Xiangpeng;HU Ronggui(Center for Excellence in Molecular Cell Science,Chinese Academy of Sciences,Shanghai 200032,China;Hangzhou Institute for Advanced Study,University of Chinese Academy of Sciences,Hangzhou 310024,China)

机构地区：[1]中国科学院分子细胞科学卓越创新中心,上海200032 [2]中国科学院大学杭州高等研究院,杭州310024

出　　处：《生命的化学》2023年第3期355-359,共5页Chemistry of Life

基　　金：脑科学重大项目科技创新2030项目(2021ZD0203900);国家自然科学基金重大研究计划集成项目(92253302);科技部“蛋白质机器与生命过程调控”重点专项(2018YFA0508200)。

摘　　要：泛素化是真核生物最普遍最重要的翻译后修饰之一,控制基因转录表达、细胞生长死亡、分子运输、代谢、发育和免疫反应等大多数生理过程。经典泛素系统的通路和机制越来越明晰,同时非经典的泛素化也逐渐被发现。本文将对经典泛素系统进行简单回顾,并且对非蛋白底物泛素化、非赖氨酸位点泛素化、非经典E3泛素连接酶等最新非经典泛素化进行阐述。Ubiquitination is one of the most common and important post-translational modifications in eukaryotes,controlling most cellular processes,such as gene transcriptional expression,cell growth and death,molecular transport,metabolism,development and immune response.In recent years,the pathways and mechanisms of the classical ubiquitin system have become increasingly clear,while non-classical ubiquitination has also been gradually discovered.Here,we will briefly review the classic ubiquitin system,and describe the latest non-classical ubiquitination,including non-protein substrate ubiquitination,non-lysine site ubiquitination and non-classical E3 ubiquitin ligases.

关 键 词：泛素 泛素化 E3泛素连接酶 

分 类 号：Q753[生物学—分子生物学]