Oxidative protein folding in the mammalian endoplasmic reticulum

Jessop, C.E., Chakravarthi, S., Watkins, R.H. and Bulleid, N.J. (2004) Oxidative protein folding in the mammalian endoplasmic reticulum. Biochemical Society Transactions, 32(5), pp. 655-658.

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Publisher's URL: http://www.biochemsoctrans.org/bst/032/0655/bst0320655.htm


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.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Bulleid, Professor Neil
Authors: Jessop, C.E., Chakravarthi, S., Watkins, R.H., and Bulleid, N.J.
Subjects:Q Science > QH Natural history > QH345 Biochemistry
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Biochemical Society Transactions

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