The redox switch: dynamic regulation of protein function by cysteine modifications.
Reactive oxygen intermediates (ROIs) and reactive nitrogen intermediates (RNIs) have now become well established as important signalling molecules in physiological settings within microorganisms, mammals and plants. These intermediates are routinely synthesised in a highly controlled and transient fashion by NADPH-dependent enzymes, which constitute key regulators of redox signalling. Mild oxidants such as hydrogen peroxide (H(2)O(2)) and especially nitric oxide (NO) signal through chemical reactions with specific atoms of target proteins that result in covalent protein modifications. Specifically, highly reactive cysteine (Cys) residues of low pK(a) are a major site of action for these intermediates. The oxidation of target Cys residues can result in a number of distinct redox-based, post-translational modifications including S-nitrosylation, S-glutathionylation; and sulphenic acid, sulphinic acid and disulphide formation. Importantly, such modifications precisely regulate protein structure and function. Cys-based redox switches are now increasingly being found to underpin many different signalling systems and regulate physiological outputs across kingdoms.
Spadaro
Davide
D
School of Biological Sciences, Institute of Molecular Plant Sciences, University of Edinburgh, Edinburgh EH9 3JR, UK.
Yun
Byung-Wook
BW
Spoel
Steven H
SH
Chu
Chengcai
C
Wang
Yi-Qin
YQ
Loake
Gary J
GJ
D003545:Cysteine / Q000378:metabolism*; D008954:Models, Biological; D009569:Nitric Oxide / Q000378:metabolism; D015538:Nitrosation; D010084:Oxidation-Reduction; D010940:Plant Proteins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D026403:S-Nitrosothiols / Q000378:metabolism; D013441:Sulfinic Acids / Q000378:metabolism; D013451:Sulfonic Acids / Q000378:metabolism
D010940:Plant Proteins; D026403:S-Nitrosothiols; D013441:Sulfinic Acids; D013451:Sulfonic Acids; D009569:Nitric Oxide; D003545:Cysteine