《生命科学》 2018, 30(4): 462-472

泛素链修饰类型研究进展

付业胜1，王　平2*，胡荣贵3*，张令强1*

(1 军事科学院军事医学科学院生命组学研究所蛋白质组学国家重点实验室，北京100850；2 同济大学医学院，上海 200092；3 中国科学院上海生物化学与细胞生物学研究所中国科学院分子细胞科学卓越中心，上海 200031)

摘　要：摘　要：泛素化修饰的蛋白质底物广泛参与蛋白质降解、胞内蛋白质转运、细胞信号转导、自噬和DNA损伤修复等重要的生物学过程。泛素化修饰包括单泛素化修饰和多泛素化修饰。因泛素分子含有7 个赖氨酸残基和1 个N 端甲硫氨酸残基，多泛素化修饰又可分为同型或异型的多聚泛素化修饰。此外，泛素分子的乙酰化修饰和磷酸化修饰大大增加了泛素链的复杂性。不同泛素链的形成往往依赖泛素连接酶或者去泛素化酶。现综述不同类型的泛素链修饰类型的编辑、识别、去除机制及其生物学功能，并讨论泛素分子自身的乙酰化和磷酸化修饰。

Research progress in ubiquitin chain linkage

FU Ye-Sheng1， WANG Ping2*， HU Rong-Gui3*， ZHANG Ling-Qiang1*

(1 State Key Laboratory of Proteomics， Beijing Institute of Lifeomics， Beijing 100850， China; 2 School of Medicine， Tongji University， Shanghai 200092， China; 3 CAS Center for Excellence in Molecular and Cell Science， Institute of Biochemistry and Cell Biology， Chinese Academy of Sciences， Shanghai 200031， China)

Abstract: Abstract: Protein ubiquitination is widely involved in multiple celluar processes， such as protein degradation， intracellular protein trafficking， cellular signaling transduction， autophagy and DNA damage responses. Ubiquitin
    modification includes monoubiquitination and polyubiquitin modification. Since ubiquitin contains seven lysine residues and one N-terminal methionine residue， the ubiquitin chains are divided into homotypic or heterotypic linkages. In addition， ubiquitin acetylation and phosphorylation improve the complexity of ubiquitin chains. There are a series of ubiquitin ligases and deubiqutinases editing different ubiquitin chains. This review focuses on different ubiquitin linkage types to discuss how they are formed， recognized and erased， and what biological functions they have. The acetylated and phosphorylated ubiquitins are also discussed.