Wilkinson K D
Department of Biochemistry, Emory University, Atlanta, Georgia 30322, USA.
FASEB J. 1997 Dec;11(14):1245-56. doi: 10.1096/fasebj.11.14.9409543.
An astounding number of important regulatory and structural proteins are subject to modification by the attachment of ubiquitin or ubiquitin-like proteins. This modification acts as a targeting signal, delivering the modified protein to different locations in the cell and modifying its activity, macromolecular interactions, or half-life. Deubiquitination, or the removal of this modification, is being recognized as an important regulatory strategy. This reaction is catalyzed by processing proteases known as deubiquitinating enzymes (DUBs). More than 60 DUBs are already known, although little is known about their biological roles. This review concentrates on recent findings and new insights into this fascinating class of enzymes.
数量惊人的重要调节蛋白和结构蛋白会通过连接泛素或类泛素蛋白而发生修饰。这种修饰充当一种靶向信号，将修饰后的蛋白传递至细胞内的不同位置，并改变其活性、大分子相互作用或半衰期。去泛素化，即去除这种修饰，正被视为一种重要的调节策略。该反应由被称为去泛素化酶（DUBs）的加工蛋白酶催化。尽管对其生物学作用了解甚少，但目前已知的去泛素化酶已超过60种。本综述着重介绍有关这类迷人酶的最新发现和新见解。
