Autoubiquitination of the Hrd1 Ligase Triggers Protein Retrotranslocation in ERAD

Misfolded proteins of the ER are retrotranslocated to the cytosol, where they are polyubiquitinated, extracted from the membrane, and degraded by the proteasome. To investigate how the ER-associated Degradation (ERAD) machinery can accomplish retrotranslocation of a misfolded luminal protein domain...

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Bibliographic Details

Published in:	Cell Vol. 166; no. 2; p. 394
Main Authors:	Baldridge, Ryan D, Rapoport, Tom A
Format:	Journal Article
Language:	English
Published:	United States 14.07.2016
Subjects:	Adenosine Triphosphatases - metabolism Cell Cycle Proteins - metabolism Endoplasmic Reticulum - metabolism Endoplasmic Reticulum-Associated Degradation Protein Folding Proteolipids - chemistry Proteolipids - metabolism Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism Ubiquitin-Protein Ligases - metabolism Ubiquitination Valosin Containing Protein
ISSN:	1097-4172, 1097-4172
Online Access:	Get more information
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