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.

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.
• Public URL: https://durham-repository.worktribe.com/output/1497470