Ubiquitin system: JAMMing in the name of the lid

被引:13
作者
Berndt, C
Bech-Otschir, D
Dubiel, W
Seeger, M
机构
[1] Humboldt Univ, Dept Surg, Div Mol Biol, D-10117 Berlin, Germany
[2] Humboldt Univ, Fac Med, Charite, Inst Biochem, D-10117 Berlin, Germany
关键词
D O I
10.1016/S0960-9822(02)01317-9
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
The isopeptide bonds formed by ubiquitin or its relatives are cleaved by hydrolases with active site cysteines. Recent studies have revealed that similar metalloprotease motifs - JAMMs - in the Rpn11 subunit of the 26S proteasome lid and in the Csn5 subunit of the COP9 signalosome are involved in deubiquitination and deneddylation, respectively.
引用
收藏
页码:R815 / R817
页数:3
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