The Requirement for Molecular Chaperones during Endoplasmic Reticulum-associated Protein Degradation Demonstrates That Protein Export and Import Are Mechanistically Distinct
Open Access
- 1 February 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (6) , 3453-3460
- https://doi.org/10.1074/jbc.274.6.3453
Abstract
No abstract availableKeywords
This publication has 64 references indexed in Scilit:
- Calnexin and Other Factors That Alter Translocation Affect the Rapid Binding of Ubiquitin to ApoB in the Sec61 ComplexPublished by Elsevier ,1998
- Role of Cue1p in Ubiquitination and Degradation at the ER SurfaceScience, 1997
- Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein.Molecular Biology of the Cell, 1996
- Degradation of 3-Hydroxy-3-methylglutaryl-CoA Reductase in Endoplasmic Reticulum Membranes Is Accelerated as a Result of Increased Susceptibility to ProteolysisJournal of Biological Chemistry, 1996
- The Human Cytomegalovirus US11 Gene Product Dislocates MHC Class I Heavy Chains from the Endoplasmic Reticulum to the CytosolCell, 1996
- Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP.The Journal of cell biology, 1996
- Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulatorsFEBS Letters, 1995
- BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast.The Journal of cell biology, 1995
- Sec61p and BiP directly facilitate polypeptide translocation into the ERCell, 1992
- Targeting and assembly of an oligomeric bacterial enterotoxoid in the endoplasmic reticulum of Saccharomyces cerevisiaeMolecular Microbiology, 1991