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.
Publication types
-
Research Support, Non-U.S. Gov't
-
Review
MeSH terms
-
Animals
-
Endoplasmic Reticulum / metabolism*
-
Humans
-
Membrane Transport Proteins / metabolism
-
Models, Biological
-
Proteasome Endopeptidase Complex / metabolism*
-
Protein Folding
-
Protein Transport
-
Proteins / chemistry
-
Proteins / metabolism
-
Ubiquitin / metabolism
-
Ubiquitin-Protein Ligase Complexes / metabolism*
-
Ubiquitin-Protein Ligases / chemistry
-
Ubiquitin-Protein Ligases / metabolism
-
Ubiquitin-Protein Ligases / physiology
-
Yeasts / metabolism
Substances
-
Membrane Transport Proteins
-
Proteins
-
Ubiquitin
-
Ubiquitin-Protein Ligase Complexes
-
Ubiquitin-Protein Ligases
-
Proteasome Endopeptidase Complex