A luminal flavoprotein in endoplasmic reticulum-associated degradation

Riemer, Jan and Appenzeller-Herzog, Christian and Johansson, Linda and Bodenmiller, Bernd and Hartmann-Petersen, Rasmus and Ellgaard, Lars. (2009) A luminal flavoprotein in endoplasmic reticulum-associated degradation. Proceedings of the National Academy of Sciences of the United States of America, Vol. 106, H. 35. pp. 14831-14836.

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Official URL: http://edoc.unibas.ch/dok/A5251913

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The quality control system of the endoplasmic reticulum (ER) discriminates between native and non-native proteins. The latter are degraded by the ER-associated degradation (ERAD) pathway. While many cytosolic and membrane components of this system are known, only few luminal players have been identified. In this study, we characterize ERFAD (ER Flavoprotein Associated with Degradation), a novel ER luminal flavoprotein that functions in ERAD. Upon knockdown of ERFAD, the degradation of the ERAD model substrate ribophorin 332 is delayed, and the overall level of polyubiquitinated cellular proteins is decreased. We also identify the ERAD components SEL1L, OS-9 and ERdj5, a known reductase of ERAD substrates, as interaction partners of ERFAD. Our data show that ERFAD facilitates the dislocation of certain ERAD substrates to the cytosol, and we discuss the findings in relation to a potential redox function of the protein.
Faculties and Departments:05 Faculty of Science > Departement Pharmazeutische Wissenschaften > Pharmazie > Molecular and Systems Toxicology (Odermatt)
UniBasel Contributors:Appenzeller, Christian
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:National Academy of Sciences
Note:Publication type according to Uni Basel Research Database: Journal article
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edoc DOI:
Last Modified:31 Dec 2015 10:47
Deposited On:22 Mar 2012 14:13

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