Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum

Tavender, T.J., Springate, J.J. and Bulleid, N.J. (2010) Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum. EMBO Journal, 29(24), pp. 4185-4197. (doi:10.1038/emboj.2010.273)

Full text not currently available from Enlighten.

Abstract

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 (H2O2). The H2O2 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 H2O2. 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 H2O2 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 H2O2.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Tavender, Dr Timothy and Bulleid, Professor Neil
Authors: Tavender, T.J., Springate, J.J., and Bulleid, N.J.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:EMBO Journal
ISSN:0261-4189
ISSN (Online):1460-2075
Published Online:05 November 2010

University Staff: Request a correction | Enlighten Editors: Update this record