Protein denitrosylation: enzymatic mechanisms and cellular functions

M Benhar, MT Forrester, JS Stamler - Nature reviews Molecular cell …, 2009 - nature.com
Nature reviews Molecular cell biology, 2009nature.com
S-Nitrosylation, the redox-based modification of Cys thiol side chains by nitric oxide, is a
common mechanism in signal transduction. Dysregulated S-nitrosylation contributes to a
range of human pathologies. New roles for protein denitrosylation in regulating S-
nitrosylation are being revealed. Recently, several denitrosylases—the enzymes that
mediate Cys denitrosylation—have been discovered, of which two enzyme systems in
particular, the S-nitrosoglutathione reductase and thioredoxin systems, have been shown to …
Abstract
S-Nitrosylation, the redox-based modification of Cys thiol side chains by nitric oxide, is a common mechanism in signal transduction. Dysregulated S-nitrosylation contributes to a range of human pathologies. New roles for protein denitrosylation in regulating S-nitrosylation are being revealed. Recently, several denitrosylases — the enzymes that mediate Cys denitrosylation — have been discovered, of which two enzyme systems in particular, the S-nitrosoglutathione reductase and thioredoxin systems, have been shown to be physiologically relevant. These highly conserved enzymes regulate signalling through multiple classes of receptors and influence diverse cellular responses. In addition, they protect from nitrosative stress in microorganisms, mammals and plants, thereby exerting profound effects on host–microbe interactions and innate immunity.
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