Ubiquitin system: JAMMing in the name of the lid.
作者信息
Berndt Christoph, Bech-Otschir Dawadschargal, Dubiel Wolfgang, Seeger Michael
机构信息
Department of Surgery, Division of Molecular Biology, Monbijoustrasse 2, 10117 Berlin, Germany.
出版信息
Curr Biol. 2002 Dec 10;12(23):R815-7. doi: 10.1016/s0960-9822(02)01317-9.
Abstract
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.
摘要
Zotero 插件