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Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48

Item Type:Article
Title:Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
Creators Name:Jarosch, E. and Taxis, C. and Volkwein, C. and Bordallo, J. and Finley, D. and Wolf, D.H. and Sommer, T.
Abstract:Endoplasmic reticulum (ER)-associated protein degradation by the ubiquitin-proteasome system requires the dislocation of substrates from the ER into the cytosol. It has been speculated that a functional ubiquitin proteasome pathway is not only essential for proteolysis, but also for the preceding export step. Here, we show that short ubiquitin chains synthesized on proteolytic substrates are not sufficient to complete dislocation; the size of the chain seems to be a critical determinant. Moreover, our results suggest that the AAA proteins of the 26S proteasome are not directly involved in substrate export. Instead, a related AAA complex Cdc48, is required for ER-associated protein degradation upstream of the proteasome.
Keywords:Adenosine Triphosphatases, Carboxypeptidases, Cathepsin A, Cell Cycle Proteins, Cell Membrane, Endoplasmic Reticulum, Fungal Proteins, Molecular Weight, Nuclear Pore Complex Proteins, Nuclear Proteins, Nucleocytoplasmic Transport Proteins, Peptide Hydrolases, Proteasome Endopeptidase Complex, Protein Transport, Saccharomyces cerevisiae Proteins, Ubiquitin, Vesicular Transport Proteins
Source:Nature Cell Biology
Publisher:Nature Publishing Group
Page Range:134-139
Date:1 February 2002
Official Publication:https://doi.org/10.1038/ncb746
PubMed:View item in PubMed

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