The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases

被引:546
作者
Jackson, PK [1 ]
Eldridge, AG
Freed, E
Furstenthal, L
Hsu, JY
Kaiser, BK
Reimann, JDR
机构
[1] Stanford Univ, Sch Med, Dept Pathol, Stanford, CA 94305 USA
[2] Stanford Univ, Sch Med, Dept Microbiol & Immunol, Stanford, CA 94305 USA
[3] Stanford Univ, Sch Med, Dept Canc Biol & Biophys, Stanford, CA 94305 USA
关键词
D O I
10.1016/S0962-8924(00)01834-1
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Recently, many nay examples of E3 ubiquitin ligases or E3 enzymes have been found to regulate a host of cellular processes. These E3 enzymes direct the formation of multiubiquitin chains on specific protein substrates, and - typically - the subsequent destruction of those proteins. We discuss how the modular architecture of E3 enzymes connects one of two distinct classes of catalytic domains to a wide range of substrate-binding domains. In one catalytic class, a HECT domain transfers ubiquitin directly to substrate bound to a non-catalytic domain. Members of the other catalytic class, found in the SCF, VBC and APC complexes, use a RING finger domain to facilitate ubiquitylation. The separable substrate-recognition domains of E3 enzymes provides a flexible means of linking a conserved ubiquitylation function to potentially thousands of ubiquitylated substrates in eukaryotic cells.
引用
收藏
页码:429 / 439
页数:11
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