Bulleid, N. J. and van Lith, M. (2014) Redox regulation in the endoplasmic reticulum. Biochemical Society Transactions, 42(4), pp. 905-908. (doi: 10.1042/BST20140065)
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Publisher's URL: http://dx.doi.org/10.1042/BST20140065
Abstract
The efficient folding, assembly and secretion of proteins from mammalian cells is a critically important process for normal cell physiology. Breakdown of the ability of cells to secrete functional proteins leads to disease pathologies caused by a lack of protein function or by cell death resulting from an aggravated stress response. Central to the folding of secreted proteins is the formation of disulfides which both aid folding and provide stability to the protein structure. For disulfides to form correctly necessitates the appropriate redox environment within the endoplasmic reticulum: too reducing and disulfides will not form, too oxidizing and non-native disulfides will not be resolved. How the endoplasmic reticulum maintains the correct redox balance is unknown. Although we have a good appreciation of the processes leading to a more oxidizing environment, our understanding of how any counterbalancing reductive pathway operates is limited. The present review looks at potential mechanisms for introducing reducing equivalents into the endoplasmic reticulum and discusses an approach to test these hypotheses.
| Item Type: | Articles |
|---|---|
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Van Lith, Dr Marcel and Bulleid, Professor Neil |
| Authors: | Bulleid, N. J., and van Lith, M. |
| College/School: | College of Medical Veterinary and Life Sciences > School of Molecular Biosciences |
| Journal Name: | Biochemical Society Transactions |
| Publisher: | Portland Press |
| ISSN: | 0300-5127 |
| ISSN (Online): | 1470-8752 |
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