The ubiquitylation machinery of the endoplasmic reticulum

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Item Type:	Review
Title:	The ubiquitylation machinery of the endoplasmic reticulum
Creators Name:	Hirsch, C., Gauss, R., Horn, S.C., Neuber, O. and Sommer, T.
Abstract:	As proteins travel through the endoplasmic reticulum (ER), a quality-control system retains newly synthesized polypeptides and supports their maturation. Only properly folded proteins are released to their designated destinations. Proteins that cannot mature are left to accumulate, impairing the function of the ER. To maintain homeostasis, the protein-quality-control system singles out aberrant polypeptides and delivers them to the cytosol, where they are destroyed by the proteasome. The importance of this pathway is evident from the growing list of pathologies associated with quality-control defects in the ER.
Keywords:	Endoplasmic Reticulum, Homeostasis, Intracellular Membranes, Proteasome Endopeptidase Complex, Protein Folding, Post-Translational Protein Processing, Proteins, Ubiquitination, Animals
Source:	Nature
ISSN:	0028-0836
Publisher:	Nature Publishing Group
Volume:	458
Number:	7237
Page Range:	453-460
Date:	26 March 2009
Official Publication:	https://doi.org/10.1038/nature07962
PubMed:	View item in PubMed

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