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A regulatory link between ER-associated protein degradation and the unfolded-protein response

Official URL:https://doi.org/10.1038/35017001
PubMed:View item in PubMed
Creators Name:Friedlander, R. and Jarosch, E. and Urban, J. and Volkwein, C. and Sommer, T.
Journal Title:Nature Cell Biology
Journal Abbreviation:Nat Cell Biol
Volume:2
Number:7
Page Range:379-384
Date:1 July 2000
Keywords:Carboxypeptidases, Cathepsin A, Cell Division, Dithiothreitol, Endoplasmic Reticulum, Genetic Epistasis, Fungal Proteins, Fungal Genes, Lethal Genes, Half-Life, Ligases, Membrane Glycoproteins, Phenotype, Protein Conformation, Protein Denaturation, Protein Folding, Protein-Serine-Threonine Kinases, Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases, Up-Regulation
Abstract:Ubiquitin conjugation during endoplasmic-reticulum-associated degradation (ERAD) depends on the activity of Ubc7. Here we show that Ubc1 acts as a further ubiquitin-conjugating enzyme in this pathway. Absence of both enzymes results in marked stabilization of an ERAD substrate and induction of the unfolded-protein response (UPR). Furthermore, basic ERAD activity is sufficient to eliminate unfolded proteins under normal conditions. However, when stress is applied, the UPR is required to increase ERAD activity. We thus demonstrate, for the first time, a regulatory loop between ERAD and the UPR, which is essential for normal growth of yeast cells.
ISSN:1465-7392
Publisher:Nature Publishing Group (U.K.)
Item Type:Article

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