Endoplasmic reticulum-associated protein degradation - one model fits all?

被引:44
作者
Hirsch, C
Jarosch, E
Sommer, T
Wolf, DH
机构
[1] Max Delbruck Ctr Mol Med, D-13092 Berlin, Germany
[2] Univ Stuttgart, Inst Biochem, D-70569 Stuttgart, Germany
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2004年 / 1695卷 / 1-3期
关键词
ERAD; endoplasmic reticulum; quality control; proteolysis; ubiquitin; proteasome; Sec61; complex; Cdc48;
D O I
10.1016/j.bbamcr.2004.10.006
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 endoplasmic reticulum (ER) is the eukaryotic organelle where most secretory proteins are folded for subsequent delivery to their Site of action. Proper folding of newly synthesized proteins is monitored by a stringent ER quality control system. This system recognizes misfolded or unassembled proteins and prevents them from reaching their final destination. Instead, they are extracted from the ER. polyubiquitinated and degraded by the cytosolic proteasome. With the identification of novel components and substrates. a more and more complex picture of this process emerges in which distinct pathways target different sets of substrates for destruction. (C) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码:215 / 223
页数:9
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