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Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds. Their primary function is to stabilize the folded structure of the protein, although disulfide bond formation can also play a regulatory role. | ỊFEBS Journal MINIREVIEW Substrate recognition by the protein disulfide isomerases Feras Hatahet and Lloyd W. Ruddock Biocenter Oulu and Department of Biochemistry University of Oulu Finland Keywords diagonal electrophoresis disulfide bond endoplasmic reticulum glutathione molecular chaperone oxidative protein folding protein folding catalyst substrate binding Correspondence L. W. Ruddock Biocenter Oulu and Department of Biochemistry PO Box 3000 90014 University of Oulu Finland Fax 358 8 553 1141 Tel 358 8 553 1683 E-mail Lloyd.ruddock@oulu.fi Received 8 June 2007 revised 27 July 2007 accepted 17 August 2007 doi 10.1111 j.1742-4658.2007.06058.x Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds. Their primary function is to stabilize the folded structure of the protein although disulfide bond formation can also play a regulatory role. Native disulfide bond formation is not trivial so it is often the rate-limiting step of protein folding both in vivo and in vitro. Complex coordinated systems of molecular chaperones and protein folding catalysts have evolved to help proteins attain their correct folded conformation. This includes a family of enzymes involved in catalyzing thiol-disulfide exchange in the endoplasmic reticulum the protein disulfide isomerase PDI family. There are now 17 reported PDI family members in the endoplasmic reticulum of human cells but the functional differentiation of these is far from complete. Despite PDI being the first catalyst of protein folding reported there is much that is still not known about its mechanisms of action. This review will focus on the interactions of the human PDI family members with substrates including recent research on identifying and characterizing their substrate-binding sites and on determining their natural substrates in vivo. Introduction The compartmentalization of cells is essential for life. Each subcellular compartment has highly defined functions .
