Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum

Benham, A.M., Van Lith, M., Sitia, R. and Braakman, I. (2013) Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum. Philosophical Transactions of the Royal Society B: Biological Sciences, 368(1617), Art. 20110403. (doi: 10.1098/rstb.2011.0403)

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Abstract

The protein folding machinery of the endoplasmic reticulum (ER) ensures that proteins entering the eukaryotic secretory pathway acquire appropriate post-translational modifications and reach a stably folded state. An important component of this protein folding process is the supply of disulfide bonds. These are introduced into client proteins by ER resident oxidoreductases, including ER oxidoreductin 1 (Ero1). Ero1 is usually considered to function in a linear pathway, by ‘donating’ a disulfide bond to protein disulfide isomerase (PDI) and receiving electrons that are passed on to the terminal electron acceptor molecular oxygen. PDI engages with a range of clients as the direct catalyst of disulfide bond formation, isomerization or reduction. In this paper, we will consider the interactions of Ero1 with PDI family proteins and chaperones, highlighting the effect that redox flux has on Ero1 partnerships. In addition, we will discuss whether higher order protein complexes play a role in Ero1 function.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Van Lith, Dr Marcel
Authors: Benham, A.M., Van Lith, M., Sitia, R., and Braakman, I.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Philosophical Transactions of the Royal Society B: Biological Sciences
Publisher:The Royal Society
ISSN:0962-8436
ISSN (Online):1471-2970
Copyright Holders:Copyright © 2013 The Authors
First Published:First published in Philosophical Transactions of the Royal Society of London Series B: Biological Sciences 368(1617): 20110403
Publisher Policy:Reproduced under a Creative Commons License

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