ER-associated degradation: Protein quality control and beyond
Open Access
- 17 March 2014
- journal article
- review article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 204 (6), 869-879
- https://doi.org/10.1083/jcb.201312042
Abstract
Even with the assistance of many cellular factors, a significant fraction of newly synthesized proteins ends up misfolded. Cells evolved protein quality control systems to ensure that these potentially toxic species are detected and eliminated. The best characterized of these pathways, the ER-associated protein degradation (ERAD), monitors the folding of membrane and secretory proteins whose biogenesis takes place in the endoplasmic reticulum (ER). There is also increasing evidence that ERAD controls other ER-related functions through regulated degradation of certain folded ER proteins, further highlighting the role of ERAD in cellular homeostasis.Keywords
This publication has 106 references indexed in Scilit:
- Deubiquitinases Sharpen Substrate Discrimination during Membrane Protein Degradation from the ERCell, 2013
- SGTA Recognizes a Noncanonical Ubiquitin-like Domain in the Bag6-Ubl4A-Trc35 Complex to Promote Endoplasmic Reticulum-Associated DegradationCell Reports, 2012
- A Ubiquitin Ligase-Associated Chaperone Holdase Maintains Polypeptides in Soluble States for Proteasome DegradationMolecular Cell, 2011
- Recognition of an ERAD-L substrate analyzed by site-specific in vivo photocrosslinkingFEBS Letters, 2011
- Rhomboid Family Pseudoproteases Use the ER Quality Control Machinery to Regulate Intercellular SignalingCell, 2011
- Cholesterol-Dependent Degradation of Squalene Monooxygenase, a Control Point in Cholesterol Synthesis beyond HMG-CoA ReductaseCell Metabolism, 2011
- Retrotranslocation of a Misfolded Luminal ER Protein by the Ubiquitin-Ligase Hrd1pCell, 2010
- Real-Time Fluorescence Detection of ERAD Substrate Retrotranslocation in a Mammalian In Vitro SystemCell, 2007
- Distinct Ubiquitin-Ligase Complexes Define Convergent Pathways for the Degradation of ER ProteinsCell, 2006
- Gp78, a Membrane-Anchored Ubiquitin Ligase, Associates with Insig-1 and Couples Sterol-Regulated Ubiquitination to Degradation of HMG CoA ReductaseMolecular Cell, 2005