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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.

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


Authors

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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Copyright Statement
© 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.







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