蛋白质泛素化修饰方式的研究进展

Progress in protein ubiquitination

泛素化是蛋白质翻译后修饰方式之一,主要通过泛素的7种赖氨酸残基(K6、K11、K27、K29、K33、K48、K63)和1种甲硫氨酸残基(Met1)发挥作用。研究发现不同的泛素链在调控蛋白质降解、DNA损伤反应和抗病毒免疫反应等中发挥重要的作用。本文总结了近几年不同类型的泛素化修饰方式在多种肿瘤的发生发展和病毒感染中的作用及其相关分子机制,为不同泛素化修饰方式的功能研究提供参考。

Ubiquitination is one of the ways of post-translational modification in proteins,which performs mainly through seven lysine residues(K6,K11,K27,K29,K33,K48,K63)and one methionine residue(M1)of ubiquitin.It has been found that different ubiquitin linkages play important roles in regulating proteasomal degradation,DNA damage response,and antiviral immunity response.In this re-view,the roles of different types of ubiquitination modifications in tumorigenesis and viral infection,and the underline molecular mechanisms in recent years are summarized,aiming to provide reference for the functional study of different ubiquitin modification.