Oxidative protein folding in the mammalian endoplasmic reticulum

C. E. Jessop, S. Chakravarthi, R. H. Watkins, N. J. Bulleid

    Research output: Contribution to journalArticlepeer-review


    Native disulphide bonds are essential for the structure and function of many membrane and secretory proteins. Disulphide bonds are formed, reduced and isomerized in the endoplasmic reticulum of mammalian cells by a family of oxidoreductases, which includes protein disulphide isomerase (PDI), ERp57, ERp72, P5 and PDIR. This review will discuss how these enzymes are maintained in either an oxidized redox state that allows them to form disulphide bonds in substrate proteins or a reduced form that allows them to perform isomerization and reduction reactions, how these opposing pathways may co-exist within the same compartment and why so many oxidoreductases exist when PDI alone can perform all three of these functions.
    Original languageEnglish
    Pages (from-to)655-658
    Number of pages3
    JournalBiochemical Society Transactions
    Issue number5
    Publication statusPublished - Nov 2004


    • Disulphide bond
    • Endoplasmic reticulum
    • Folding
    • Glutathione
    • Oxidoreductase
    • Protein disulphide isomerase


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