Kerscher Oliver, Felberbaum Rachael, Hochstrasser Mark
Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA.
Annu Rev Cell Dev Biol. 2006;22:159-80. doi: 10.1146/annurev.cellbio.22.010605.093503.
Following the discovery of protein modification by the small, highly conserved ubiquitin polypeptide, a number of distinct ubiquitin-like proteins (Ubls) have been found to function as protein modifiers as well. These Ubls, which include SUMO, ISG15, Nedd8, and Atg8, function as critical regulators of many cellular processes, including transcription, DNA repair, signal transduction, autophagy, and cell-cycle control. A growing body of data also implicates the dysregulation of Ubl-substrate modification and mutations in the Ubl-conjugation machinery in the etiology and progression of a number of human diseases. The primary aim of this review is to summarize the latest developments in our understanding of the different Ubl-protein modification systems, including the shared and unique features of these related pathways.
在发现小的、高度保守的泛素多肽可对蛋白质进行修饰之后，人们又发现了许多不同的类泛素蛋白（Ubls）也能作为蛋白质修饰剂发挥作用。这些Ubls包括SUMO、ISG15、Nedd8和Atg8，它们是许多细胞过程的关键调节因子，这些过程包括转录、DNA修复、信号转导、自噬和细胞周期控制。越来越多的数据还表明，Ubl-底物修饰的失调以及Ubl-缀合机制中的突变与多种人类疾病的病因和进展有关。本综述的主要目的是总结我们对不同Ubl-蛋白质修饰系统理解的最新进展，包括这些相关途径的共同特征和独特特征。
