摘要
泛素(ubiquitin,Ub)是一类高度保守的小蛋白,可与靶蛋白的赖氨酸残基共价连接,形成多聚泛素链行使功能.类似于泛素化修饰过程,小泛素相关修饰物(small ubiquitin-related modifier,SUMO)也可以共价修饰靶蛋白的赖氨酸残基,从而影响靶蛋白的定位、稳定性以及蛋白间的相互作用,发挥重要的生理功能.尽管在多数情况下,靶蛋白发生的是单SUMO化修饰,但最近研究发现,SUMO依赖自身的赖氨酸也可以形成多聚链.与单SUMO化修饰不同的是,多聚SUMO化修饰的靶蛋白可以进一步被泛素化修饰,进而诱导靶蛋白的降解.这是一种新的、特殊的化学修饰形式,弄清它的生理功能,对于了解细胞的生长、分化以及凋亡等生理过程将具有重要的意义.本文将就此方面的最新研究进展做一综述.
Ubiquitin is a highly conserved small protein that functioned by covalently interact with the lysines on target proteins and forms poly-ubiquitin chains.The small ubiquitin-related modifier（SUMO）also covalently modifies the lysines in target proteins to regulate their localization,stability,interactions and physiological functions.The interaction with single SUMO is predominant,yet it has recently been found that SUMO could also form poly-ubiquitin chains at its inner lysines.Different from single-SUMOylation,proteins with poly-SUMO chains could be further modified by ubiquitin,then targeted for protein degradation.To find out the physiological function in cell growth,differentiation or apoptosis of poly-SUMOylation will be important.This review will introduce the latest researches about poly-SUMOylation.
出处
《中国生物化学与分子生物学报》
CAS
CSCD
北大核心
2009年第11期977-982,共6页
Chinese Journal of Biochemistry and Molecular Biology
基金
国家自然科学基金(No.30670409
30771221)
科技部国家高技术研究发展计划资助项目(863计划
No.2006AA02Z120)~~
