Yos9p Assists in the Degradation of Certain Nonglycosylated Proteins from the Endoplasmic Reticulum

Overview

Journal Mol Biol Cell

Specialties Cell Biology
Molecular Biology

Date 2011 Jul 9

PMID 21737688

Citations 24

Authors

Laura A Jaenicke

Holger Brendebach

Matthias Selbach

Christian Hirsch

Affiliations

Soon will be listed here.

Abstract

The HRD ubiquitin ligase recognizes and ubiquitylates proteins of the endoplasmic reticulum that display structural defects. Here, we apply quantitative proteomics to characterize the substrate spectrum of the HRD complex. Among the identified substrates is Erg3p, a glycoprotein involved in sterol synthesis. We characterize Erg3p and demonstrate that the elimination of Erg3p requires Htm1p and Yos9p, two proteins that take part in the glycan-dependent turnover of aberrant proteins. We further show that the HRD ligase also mediates the breakdown of Erg3p and CPY* engineered to lack N-glycans. The degradation of these nonglycosylated substrates is enhanced by a mutant variant of Yos9p that has lost its affinity for oligosaccharides, indicating that Yos9p has a previously unrecognized role in the quality control of nonglycosylated proteins.

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