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Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum
Disulphide formation in the endoplasmic reticulum (ER) is catalysed by members of the protein disulphide isomerase (PDI) family. These enzymes can be oxidized by the flavoprotein ER oxidoreductin 1 (Ero1), which couples disulphide formation with reduction of oxygen to form hydrogen peroxide (H(2)O(2...
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Formato: | Texto |
Lenguaje: | English |
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Nature Publishing Group
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3018787/ https://www.ncbi.nlm.nih.gov/pubmed/21057456 http://dx.doi.org/10.1038/emboj.2010.273 |
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author | Tavender, Timothy J Springate, Jennifer J Bulleid, Neil J |
author_facet | Tavender, Timothy J Springate, Jennifer J Bulleid, Neil J |
author_sort | Tavender, Timothy J |
collection | PubMed |
description | Disulphide formation in the endoplasmic reticulum (ER) is catalysed by members of the protein disulphide isomerase (PDI) family. These enzymes can be oxidized by the flavoprotein ER oxidoreductin 1 (Ero1), which couples disulphide formation with reduction of oxygen to form hydrogen peroxide (H(2)O(2)). The H(2)O(2) produced can be metabolized by ER-localized peroxiredoxin IV (PrxIV). Continuous catalytic activity of PrxIV depends on reduction of a disulphide within the active site to form a free thiol, which can then react with H(2)O(2). Here, we demonstrate that several members of the PDI family are able to directly reduce this PrxIV disulphide and in the process become oxidized. Furthermore, we show that altering cellular expression of these proteins within the ER influences the efficiency with which PrxIV can be recycled. The oxidation of PDI family members by PrxIV is a highly efficient process and demonstrates how oxidation by H(2)O(2) can be coupled to disulphide formation. Oxidation of PDI by PrxIV may therefore increase efficiency of disulphide formation by Ero1 and also allows disulphide formation via alternative sources of H(2)O(2). |
format | Text |
id | pubmed-3018787 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-30187872011-02-09 Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum Tavender, Timothy J Springate, Jennifer J Bulleid, Neil J EMBO J Article Disulphide formation in the endoplasmic reticulum (ER) is catalysed by members of the protein disulphide isomerase (PDI) family. These enzymes can be oxidized by the flavoprotein ER oxidoreductin 1 (Ero1), which couples disulphide formation with reduction of oxygen to form hydrogen peroxide (H(2)O(2)). The H(2)O(2) produced can be metabolized by ER-localized peroxiredoxin IV (PrxIV). Continuous catalytic activity of PrxIV depends on reduction of a disulphide within the active site to form a free thiol, which can then react with H(2)O(2). Here, we demonstrate that several members of the PDI family are able to directly reduce this PrxIV disulphide and in the process become oxidized. Furthermore, we show that altering cellular expression of these proteins within the ER influences the efficiency with which PrxIV can be recycled. The oxidation of PDI family members by PrxIV is a highly efficient process and demonstrates how oxidation by H(2)O(2) can be coupled to disulphide formation. Oxidation of PDI by PrxIV may therefore increase efficiency of disulphide formation by Ero1 and also allows disulphide formation via alternative sources of H(2)O(2). Nature Publishing Group 2010-12-15 2010-11-05 /pmc/articles/PMC3018787/ /pubmed/21057456 http://dx.doi.org/10.1038/emboj.2010.273 Text en Copyright © 2010, European Molecular Biology Organization http://creativecommons.org/licenses/by-nc-sa/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution Noncommercial Share Alike 3.0 Unported License, which allows readers to alter, transform, or build upon the article and then distribute the resulting work under the same or similar license to this one. The work must be attributed back to the original author and commercial use is not permitted without specific permission. |
spellingShingle | Article Tavender, Timothy J Springate, Jennifer J Bulleid, Neil J Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum |
title | Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum |
title_full | Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum |
title_fullStr | Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum |
title_full_unstemmed | Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum |
title_short | Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum |
title_sort | recycling of peroxiredoxin iv provides a novel pathway for disulphide formation in the endoplasmic reticulum |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3018787/ https://www.ncbi.nlm.nih.gov/pubmed/21057456 http://dx.doi.org/10.1038/emboj.2010.273 |
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