Diversity of degradation signals in the ubiquitin-proteasome system

被引:640
作者
Ravid, Tommer [1 ]
Hochstrasser, Mark [2 ]
机构
[1] Hebrew Univ Jerusalem, Dept Biol Chem, IL-91904 Jerusalem, Israel
[2] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1038/nrm2468
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The ubiquitin-proteasome system degrades an enormous variety of proteins that contain specific degradation signals, or 'degrons'. Besides the degradation of regulatory proteins, almost every protein suffers from sporadic biosynthetic errors or misfolding. Such aberrant proteins can be recognized and rapidly degraded by cells. Structural and functional data on a handful of degrons allow several generalizations regarding their mechanism of action. We focus on different strategies of degron recognition by the ubiquitin system, and contrast regulatory degrons that are subject to signalling-dependent modification with those that are controlled by protein folding or assembly, as frequently occurs during protein quality control.
引用
收藏
页码:679 / U25
页数:12
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