Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome

被引：461

作者：

Wilkinson, KD ^{[1
]}

机构：

[1] Emory Univ, Sch Med, Dept Biochem, Atlanta, GA 30322 USA

来源：

SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY | 2000年 / 11卷 / 03期

关键词：

deubiquitinating enzymes; proteolysis; regulation; ubiquitin; ubiquitin ligase;

D O I：

10.1006/scdb.2000.0164

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The post-translational modification of proteins by covalent attachment of ubiquitin targets these proteins for degradation by the proteasome. An astounding number of proteins are involved in ubiquitination and deubiquitination of proteins. The pathways are combinatorial, and selectivity of proteolysis will depend strongly on the exact combination of ubiquitinating- and deubiquitinating enzymes present at any time. lit addition to temporal control, it is likely that these modifications are also regulated spatially. In this review, we discuss the regulation of ubiquitination by enzymes of this pathway and highlight some of the outstanding problems in understanding this regulation.

引用

页码：141 / 148

页数：8

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