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

页码：979 / 981

页数：3

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