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Role of Cue1p in ubiquitination and degradition at the ER surface

Item Type:Article
Title:Role of Cue1p in ubiquitination and degradition at the ER surface
Creators Name:Biederer, T. and Volkwein, C. and Sommer, T.
Abstract:Endoplasmic reticulum (ER) degradation of aberrant proteins is mediated by the ubiquitin-proteasome pathway. Here, a membrane-bound component of the ubiquitin system, Cue1p, was identified. It was shown to recruit the soluble ubiquitin-conjugating enzyme Ubc7p to the ER membrane. In the absence of Cue1p, unassembled and thus cytosolically mislocalized Ubc7p was unable to participate in ER degradation or in the turnover of soluble non-ER proteins. Moreover, ubiquitination by Cue1p-assembled Ubc7p and Ubc6p was a prerequisite for retrograde transport of lumenal substrates out of the ER, which suggests that ubiquitination is mechanistically integrated into the ER degradation process.
Keywords:Amino Acid Sequence, Biological Transport, Carboxypeptidases, Carrier Proteins, Cathepsin A, Cysteine Endopeptidases, Cytosol, Endoplasmic Reticulum, Intracellular Membranes, Ligases, Membrane Proteins, Molecular Sequence Data, Multienzyme Complexes, Proteasome Endopeptidase Complex, Saccharomyces cerevisiae Proteins, Ubiquitin-Conjugating Enzymes, Ubiquitins, Yeasts
Source:Science
ISSN:0036-8075
Publisher:American Association for the Advancement of Science (U.S.A.)
Volume:278
Number:5344
Page Range:1806-1809
Date:5 December 1997
Official Publication:https://doi.org/10.1126/science.278.5344.1806
PubMed:View item in PubMed

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