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

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 bond...

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Detalles Bibliográficos
Autores principales: Benham, Adam M., van Lith, Marcel, Sitia, Roberto, Braakman, Ineke
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3638393/
https://www.ncbi.nlm.nih.gov/pubmed/23530257
http://dx.doi.org/10.1098/rstb.2011.0403
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author Benham, Adam M.
van Lith, Marcel
Sitia, Roberto
Braakman, Ineke
author_facet Benham, Adam M.
van Lith, Marcel
Sitia, Roberto
Braakman, Ineke
author_sort Benham, Adam M.
collection PubMed
description 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.
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spelling pubmed-36383932013-05-05 Ero1–PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum Benham, Adam M. van Lith, Marcel Sitia, Roberto Braakman, Ineke Philos Trans R Soc Lond B Biol Sci Articles 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. The Royal Society 2013-05-05 /pmc/articles/PMC3638393/ /pubmed/23530257 http://dx.doi.org/10.1098/rstb.2011.0403 Text en http://creativecommons.org/licenses/by/3.0/ © 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.
spellingShingle Articles
Benham, Adam M.
van Lith, Marcel
Sitia, Roberto
Braakman, Ineke
Ero1–PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
title Ero1–PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
title_full Ero1–PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
title_fullStr Ero1–PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
title_full_unstemmed Ero1–PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
title_short Ero1–PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
title_sort ero1–pdi interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3638393/
https://www.ncbi.nlm.nih.gov/pubmed/23530257
http://dx.doi.org/10.1098/rstb.2011.0403
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