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The role of redox in signal transduction

Hancock, John T.

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Abstract

© Springer Science+Business Media, LLC, part of Springer Nature 2019. It is the functioning of efficient cell signaling which is vital for the survival of cells, whether it is a simple prokaryote or a complex eukaryote, including both animals and plants. Over many years various components have been identified and recognized as crucial for the transduction of signals in cells, including small organic molecules and ions. Many of the mechanisms allow for a relatively rapid switching of signals, on or off, with common examples being the G proteins and protein phosphorylation. However, it has become apparent that other amino acid modifications are also vitally important. This includes reactions with nitric oxide, for example S-nitrosation (S-nitrosylation), and, of particular relevance here, oxidation of cysteine residues. Such oxidation will be dependent on the redox status of the intracellular environment in which that protein resides, and this will in turn be dictated by the presence of pro-oxidants and antioxidants, either produced by the cell itself or from the cell’s environment. Here, the chemistry of redox modification of amino acids is introduced, and a general overview of the role of redox in mediating signal transduction is given.

Publication Date Jan 1, 2019
Journal Methods in Molecular Biology
Peer Reviewed Not Peer Reviewed
Volume 1990
Pages 1-11
Series Title Methods in Molecular Biology
Series Number 1990
Book Title Redox-Mediated Signal Transduction
ISBN 9781493994618
APA6 Citation Hancock, J. T. (2019). The role of redox in signal transduction. In J. T. Hancock, & M. E. Conway (Eds.), Redox-Mediated Signal Transduction, (1-11). Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9463-2_1
DOI https://doi.org/10.1007/978-1-4939-9463-2_1
Keywords cysteine modification, hydrogen peroxide, hydrogen sulfide, nitric oxide, redox S-nitrosation, signal transduction, thiol modifications
Publisher URL https://doi.org/10.1007/978-1-4939-9463-2_1
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