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.; Braakman, I.

doi:10.1098/rstb.2011.0403

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.; Braakman, I.

Authors

Professor Adam Benham adam.benham@durham.ac.uk
Professor

M. van Lith

R. Sitia

I. Braakman

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.

Citation

Benham, A., van Lith, M., Sitia, R., & 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), Article 20110403. https://doi.org/10.1098/rstb.2011.0403

Journal Article Type	Article
Publication Date	Mar 1, 2013
Deposit Date	Feb 11, 2013
Publicly Available Date	Jan 3, 2014
Journal	Philosophical Transactions of the Royal Society B: Biological Sciences
Print ISSN	0962-8436
Electronic ISSN	1471-2970
Publisher	The Royal Society
Peer Reviewed	Peer Reviewed
Volume	368
Issue	1617
Article Number	20110403
DOI	https://doi.org/10.1098/rstb.2011.0403
Keywords	Chaperone, Endoplasmic reticulum, Protein folding, Redox Disulfide bond.

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© 2013 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0/, which permits unrestricted use, provided the original author and source are credited.