小泛素样修饰（SUMO）化与去小泛素样修饰（SUMO）化：与生命过程的较量
SUMOylation and De-SUMOylation: wrestling with life's processes.
作者信息
Yeh Edward T H
机构信息
Department of Cardiology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030, USA.
出版信息
J Biol Chem. 2009 Mar 27;284(13):8223-7. doi: 10.1074/jbc.R800050200. Epub 2008 Nov 13.
Abstract
The small ubiquitin-like modifier (SUMO) is a ubiquitin-like protein that covalently modifies a large number of cellular proteins. SUMO modification has emerged as an important regulatory mechanism for protein function and localization. SUMOylation is a dynamic process that is mediated by activating (E1), conjugating (E2), and ligating (E3) enzymes and readily reversed by a family of ubiquitin-like protein-specific proteases (Ulp) in yeast and sentrin/SUMO-specific proteases (SENP) in human. This review will focus on the de-SUMOylating enzymes with special attention to their biological function.
摘要
小泛素样修饰蛋白（SUMO）是一种类泛素蛋白，可共价修饰大量细胞蛋白。SUMO修饰已成为蛋白质功能和定位的重要调控机制。SUMO化是一个动态过程，由激活酶（E1）、缀合酶（E2）和连接酶（E3）介导，并可被酵母中的泛素样蛋白特异性蛋白酶家族（Ulp）和人类中的sentrin/SUMO特异性蛋白酶（SENP）轻易逆转。本综述将聚焦于去SUMO化酶，特别关注它们的生物学功能。
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