Helmholtz Gemeinschaft

Search
Browse
Statistics
Feeds

ERAD: the long road to destruction

Official URL:https://doi.org/10.1038/ncb0805-766
PubMed:View item in PubMed
Creators Name:Meusser, B. and Hirsch, C. and Jarosch, E. and Sommer, T.
Journal Title:Nature Cell Biology
Journal Abbreviation:Nat Cell Biol
Volume:7
Number:8
Page Range:766-772
Date:August 2005
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
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.
ISSN:1465-7392
Publisher:Nature Publishing Group (U.K.)
Item Type:Review

Repository Staff Only: item control page

Open Access
MDC Library