Endoplasmic reticulum-associated protein degradation - one model fits all?

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Item Type:	Review
Title:	Endoplasmic reticulum-associated protein degradation - one model fits all?
Creators Name:	Hirsch, C., Jarosch, E., Sommer, T. and Wolf, D.H.
Abstract:	The endoplasmic reticulum (ER) is the eukaryotic organelle where most secretory proteins are folded for subsequent delivery to their site of action. Proper folding of newly synthesized proteins is monitored by a stringent ER quality control system. This system recognizes misfolded or unassembled proteins and prevents them from reaching their final destination. Instead, they are extracted from the ER, polyubiquitinated and degraded by the cytosolic proteasome. With the identification of novel components and substrates, a more and more complex picture of this process emerges in which distinct pathways target different sets of substrates for destruction.
Keywords:	Cdc48 Complex, Endoplasmic Reticulum, ERAD, Proteasome, Proteolysis, Quality Control, Sec61 Complex, Ubiquitin
Source:	Biochimica et Biophysica Acta - Molecular Cell Research
ISSN:	0167-4889
Publisher:	Elsevier
Volume:	1695
Number:	1-3
Page Range:	215-223
Date:	1 January 2004
Official Publication:	https://doi.org/10.1016/j.bbamcr.2004.10.006
PubMed:	View item in PubMed

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