The ubiquitylation machinery of the endoplasmic reticulum

被引：290

作者：

Hirsch, Christian ^{[1
]}

Gauss, Robert ^{[1
]}

Horn, Sabine C. ^{[1
]}

Neuber, Oliver ^{[1
]}

Sommer, Thomas ^{[1
]}

机构：

[1] Max Delbruck Ctr Mol Med, D-13125 Berlin, Germany

来源：

NATURE | 2009年 / 458卷 / 7237期

关键词：

ER-ASSOCIATED DEGRADATION; UNFOLDED PROTEIN RESPONSE; ANCHORED UBIQUITIN LIGASE; MANNOSIDASE-LIKE PROTEIN; N-LINKED GLYCANS; QUALITY-CONTROL; MEMBRANE-PROTEIN; SACCHAROMYCES-CEREVISIAE; MISFOLDED GLYCOPROTEINS; ALPHA-MANNOSIDASE;

D O I：

10.1038/nature07962

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

As proteins travel through the endoplasmic reticulum (ER), a quality-control system retains newly synthesized polypeptides and supports their maturation. Only properly folded proteins are released to their designated destinations. Proteins that cannot mature are left to accumulate, impairing the function of the ER. To maintain homeostasis, the protein-quality-control system singles out aberrant polypeptides and delivers them to the cytosol, where they are destroyed by the proteasome. The importance of this pathway is evident from the growing list of pathologies associated with quality-control defects in the ER.

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页码：453 / 460

页数：8

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