Item Type: | Review |
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Title: | ERAD: the long road to destruction |
Creators Name: | Meusser, B., Hirsch, C., Jarosch, E. and Sommer, T. |
Abstract: | Endoplasmic reticulum (ER)-associated protein degradation (ERAD) eliminates misfolded or unassembled proteins from the ER. ERAD targets are selected by a quality control system within the ER lumen and are ultimately destroyed by the cytoplasmic ubiquitin-proteasome system (UPS). The spatial separation between substrate selection and degradation in ERAD requires substrate transport from the ER to the cytoplasm by a process termed dislocation. In this review, we will summarize advances in various aspects of ERAD and discuss new findings on how substrate dislocation is achieved. |
Keywords: | Endoplasmic Reticulum, Membrane Transport Proteins, Biological Models, Proteasome Endopeptidase Complex, Protein Folding, Protein Transport, Proteins, Ubiquitin, Ubiquitin-Protein Ligase Complexes, Ubiquitin-Protein Ligases, Yeasts, Animals |
Source: | Nature Cell Biology |
ISSN: | 1465-7392 |
Publisher: | Nature Publishing Group |
Volume: | 7 |
Number: | 8 |
Page Range: | 766-772 |
Date: | August 2005 |
Official Publication: | https://doi.org/10.1038/ncb0805-766 |
PubMed: | View item in PubMed |
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