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A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery

Official URL:https://doi.org/10.1038/ncb1445
PubMed:View item in PubMed
Creators Name:Gauss, R. and Jarosch, E. and Sommer, T. and Hirsch, C.
Journal Title:Nature Cell Biology
Journal Abbreviation:Nat Cell Biol
Volume:8
Number:8
Page Range:849-854
Date:August 2006
Keywords:Western Blotting, Carrier Proteins, Endoplasmic Reticulum, Hydrolysis, Immunoprecipitation, Membrane Glycoproteins, Plasmids, Protein Binding, Protein Conformation, Protein Folding, Saccharomyces Cerevisiae, Saccharomyces Cerevisiae Proteins, Ubiquitin-Protein Ligases
Abstract:A quality-control system surveys the lumen of the endoplasmic reticulum for terminally misfolded proteins. Polypeptides singled out by this system are ultimately degraded by the cytosolic ubiquitin-proteasome pathway. Key components of both the endoplasmic reticulum quality-control system and the degradation machinery have been identified, but a connection between the two systems has remained elusive. Here, we report an association between the endoplasmic reticulum quality-control lectin Yos9p and Hrd3p, a component of the ubiquitin-proteasome system that links these pathways. We identify designated regions in the luminal domain of Hrd3p that interact with Yos9p and the ubiquitin ligase Hrd1p. Binding of misfolded proteins occurs through Hrd3p, suggesting that Hrd3p recognises proteins that deviate from their native conformation, whereas Yos9p ensures that only terminally misfolded polypeptides are degraded.
ISSN:1465-7392
Publisher:Nature Publishing Group (U.K.)
Item Type:Article

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