Disulfide bond formation in the mammalian endoplasmic reticulum

Bulleid, N.J. (2012) Disulfide bond formation in the mammalian endoplasmic reticulum. Cold Spring Harbor Perspectives in Biology, 4(11), a013219-a013219. (doi:10.1101/cshperspect.a013219)

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Abstract

The formation of disulfide bonds between cysteine residues occurs during the folding of many proteins that enter the secretory pathway. As the polypeptide chain collapses, cysteines brought into proximity can form covalent linkages during a process catalyzed by members of the protein disulfide isomerase family. There are multiple pathways in mammalian cells to ensure disulfides are introduced into proteins. Common requirements for this process include a disulfide exchange protein and a protein oxidase capable of forming disulfides de novo. In addition, any incorrect disulfides formed during the normal folding pathway are removed in a process involving disulfide exchange. The pathway for the reduction of disulfides remains poorly characterized. This work will cover the current knowledge in the field and discuss areas for future investigation.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Bulleid, Professor Neil
Authors: Bulleid, N.J.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Cold Spring Harbor Perspectives in Biology
Publisher:Cold Spring Harbor Laboratory Press
ISSN:1943-0264
ISSN (Online):1943-0264

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