摘要
蛋白质的翻译后修饰对调节蛋白质的功能活性和定位以及调控细胞周期进程和细胞分化都起着非常重要的作用,其中小泛素样修饰蛋白(SUMO)化修饰是一个可以由SUMO特异性蛋白酶(SENPs)家族逆转的高度动态的过程。SENPs能够从与SUMO连接的靶蛋白上催化去除SUMO,以及从它的前体蛋白上裂解SUMO;同时,此家族部分成员还参与SUMO的成熟活化过程;因此,去SUMO化修饰对于调节SUMO连接蛋白的功能及活性与SUMO化同样重要。本文就SENPs家族的结构及生物学特性作一综述。
Post-translational modification of proteins plays a very important role in regulating function, activity and positioning of proteins, as well as the progression of cell cycle and cell differentiation. SUMOylation (SUMO, small ubiquitin-like modifier) is a highly dynamic process which can be reserved by SUMO specific proteases (SENPs) family. SENPs can catalyze and remove SUMO from SUMO-connecting target proteins, as well as from their precursor proteins. Furthermore, some members of this family are involved in the maturation and activation of SUMO. Thus, deSUMOylation is as important as SUMOylation to the regulation of function and activity of SUMO-connecting proteins. This paper reviews the structure and biological characteristics of SENPs family.
出处
《上海交通大学学报(医学版)》
CAS
CSCD
北大核心
2014年第11期1683-1687,共5页
Journal of Shanghai Jiao tong University:Medical Science
基金
国家自然科学基金(81302086)
高等学校博士学科点专项科研基金(20130073120007)
上海市科技人才计划项目浦江人才A类项目(13PJ1406100)~~