A systematic search for endoplasmic reticulum (ER) membrane-associated RING finger proteins identifies Nixin/ZNRF4 as a regulator of calnexin stability and ER homeostasis
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 1195213
Author(s) Neutzner, Albert; Neutzner, Melanie; Benischke, Anne-Sophie; Ryu, Seung-Wook; Frank, Stephan; Youle, Richard J.; Karbowski, Mariusz
Author(s) at UniBasel Frank, Stephan
Neutzner, Albert
Year 2011
Title A systematic search for endoplasmic reticulum (ER) membrane-associated RING finger proteins identifies Nixin/ZNRF4 as a regulator of calnexin stability and ER homeostasis
Journal Journal of biological chemistry
Volume 286
Number 10
Pages / Article-Number 8633-43
Keywords Calnexin/genetics/*metabolism; DNA-Binding Proteins/genetics/*metabolism; Down-Regulation/*physiology; Endoplasmic Reticulum/genetics/*metabolism; Glycosylation; HeLa Cells; Humans; Protein Stability
Abstract

To identify novel regulators of endoplasmic reticulum (ER)-linked protein degradation and ER function, we determined the entire inventory of membrane-spanning RING finger E3 ubiquitin ligases localized to the ER. We identified 24 ER membrane-anchored ubiquitin ligases and found Nixin/ZNRF4 to be central for the regulation of calnexin turnover. Ectopic expression of wild type Nixin induced a dramatic down-regulation of the ER-localized chaperone calnexin that was prevented by inactivation of the Nixin RING domain. Importantly, Nixin physically interacts with calnexin in a glycosylation-independent manner, induces calnexin ubiquitination, and p97-dependent degradation, indicating an ER-associated degradation-like mechanism of calnexin turnover.

Publisher American Society of Biological Chemists
ISSN/ISBN 0021-9258
edoc-URL http://edoc.unibas.ch/dok/A6005399
Full Text on edoc No
Digital Object Identifier DOI 10.1074/jbc.M110.197459
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/21205830
ISI-Number WOS:000288013300089
Document type (ISI) Journal Article
 
   

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