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 > School of Molecular Biosciences |
| 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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