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

Adam M. Benham, Marcel van Lith, Roberto Sitia, Ineke Braakman

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)20110403
Number of pages1
JournalPhilosophical transactions of the Royal Society of London. Series B: Biological sciences
Volume368
Issue number1617
DOIs
Publication statusPublished - May 5 2013

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ASJC Scopus subject areas

  • Medicine(all)

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