Disulphide bonds are critical for the maturation and stability of secretory and cell-surface proteins. In eukaryotic cells, disulphide bonds are introduced in the ER (endoplasmic reticulum), where the redox conditions are optimal to support their formation. Yet, the correct pairing of cysteine residues is not simple and often requires the assistance of redox-active proteins. The enzymes of the thiol-disulphide oxidoreductase family catalyse oxidation, reduction and isomerization, and thereby play important roles for the folding of many proteins. To allow all three redox reactions to take place concurrently in the same compartment, specific protein–protein interactions regulate the function of individual enzymes, while a careful balance of the ER redox environment is maintained. At the same time, the system must be capable of responding to changes in the cellular conditions, caused, for instance, by oxidative stress and protein misfolding. This review presents recent progress in understanding how ER redox conditions are regulated and how protein disulphides are formed in the ER of mammalian cells.
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November 2004
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Conference Article|
October 26 2004
Catalysis of disulphide bond formation in the endoplasmic reticulum
L. Ellgaard
L. Ellgaard
1
1Institute of Biochemistry, Swiss Federal Institute of Technology (ETH), ETH Hoenggerberg, CH-8093 Zurich, Switzerland
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Publisher: Portland Press Ltd
Received:
June 21 2004
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2004 The Biochemical Society
2004
Biochem Soc Trans (2004) 32 (5): 663–667.
Article history
Received:
June 21 2004
Citation
L. Ellgaard; Catalysis of disulphide bond formation in the endoplasmic reticulum. Biochem Soc Trans 1 November 2004; 32 (5): 663–667. doi: https://doi.org/10.1042/BST0320663
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