Making the cut: intramembrane cleavage by a rhomboid protease promotes ERAD

被引：17
|
作者：
Greenblatt, Ethan J. [1 ]
Olzmann, James A. [2 ]
Kopito, Ron R. [2 ]
机构：
[1] Carnegie Inst Sci, Dept Embryol, Howard Hughes Med Inst, Res Labs, Baltimore, MD 21210 USA
[2] Stanford Univ, Dept Biol, Stanford, CA 94305 USA
来源：
NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2012年 / 19卷 / 10期
关键词：
ENDOPLASMIC-RETICULUM; QUALITY-CONTROL; DEGRADATION; MEMBRANE; DOMAIN; DISLOCATION; IRHOM2; TACE;
D O I：
10.1038/nsmb.2398
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：
Endoplasmic reticulum-associated degradation (ERAD) is a cellular protein quality-control process that disposes of proteasomal substrates from the early secretory pathway. Recent work shows that the endoplasmic reticulum-resident rhomboid protease RHBDL4 facilitates ERAD by recognizing and cleaving integral membrane substrates. The work indicates that intramembrane proteolysis may have a general role in the extraction of misfolded membrane proteins from the endoplasmic reticulum.
引用
收藏
页码：979 / 981
页数：3
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