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

• Timothy J Tavender ^[1] ; Jennifer J Springate ^[2] ; Neil J Bulleid ^[1]
  1. [1] University of Glasgow

     University of Glasgow

     Reino Unido

     
  2. [2] University of Manchester

     University of Manchester

     Reino Unido

     
• Localización: EMBO journal: European Molecular Biology Organization, ISSN 0261-4189, Vol. 29, Nº. 24, 2010, págs. 4185-4197
• Idioma: inglés
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• Resumen

  • Ero1 is thought to be the only oxidase that mediates the re-oxidation of protein disulphide isomerases (PDIs) during oxidative protein folding in the ER. This study reveals that peroxiredoxin IV can also directly oxidize PDI-family members and thus act as a second source of oxidizing equivalents for disulphide-bond formation in the ER.