共 59 条
RINGs hold the key to ubiquitin transfer
被引:154
作者:

Budhidarmo, Rhesa
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h-index: 0
机构:
Univ Otago, Dept Biochem, Dunedin 9054, New Zealand Univ Otago, Dept Biochem, Dunedin 9054, New Zealand

Nakatani, Yoshio
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h-index: 0
机构:
Univ Otago, Dept Biochem, Dunedin 9054, New Zealand Univ Otago, Dept Biochem, Dunedin 9054, New Zealand

Day, Catherine L.
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h-index: 0
机构:
Univ Otago, Dept Biochem, Dunedin 9054, New Zealand Univ Otago, Dept Biochem, Dunedin 9054, New Zealand
机构:
[1] Univ Otago, Dept Biochem, Dunedin 9054, New Zealand
关键词:
U-BOX;
CONJUGATING ENZYME;
CRYSTAL-STRUCTURE;
ALLOSTERIC ACTIVATION;
MECHANISTIC INSIGHT;
ANTAGONISTS INDUCE;
LIGASE CHIP;
COMPLEX;
UBIQUITYLATION;
REVEALS;
D O I:
10.1016/j.tibs.2011.11.001
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Ubiquitylation, the covalent modification of proteins by the addition of ubiquitin, relies on a cascade of enzymes that culminates in an E3 ligase that promotes the transfer of ubiquitin from an E2 enzyme to the target protein. The most prevalent E3 ligases contain a type of zinc-finger domain called RING, and although an essential role for the RING domain in ubiquitin transfer is widely accepted, the molecular mechanism by which this is achieved remains uncertain. In this review, we highlight recent studies that have suggested that the RING domain modulates the stability of the E2 similar to ubiquitin conjugate so that catalysis is promoted. We also review the role of RING dimerisation and emphasise the importance of studying RING domains in the context of the full-length protein.
引用
收藏
页码:58 / 65
页数:8
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