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Review
. 2012 Feb 10;287(7):4411-8.
doi: 10.1074/jbc.R111.285742. Epub 2011 Dec 6.

Regulation by S-nitrosylation of protein post-translational modification

Douglas T Hess  1 , Jonathan S Stamler
Affiliations
Review

Regulation by S-nitrosylation of protein post-translational modification

Douglas T Hess et al. J Biol Chem. .

Abstract

Protein post-translational modification by S-nitrosylation conveys a ubiquitous influence of nitric oxide on signal transduction in eukaryotic cells. The wide functional purview of S-nitrosylation reflects in part the regulation by S-nitrosylation of the principal protein post-translational modifications that play a role in cell signaling, including phosphorylation, acetylation, ubiquitylation and related modifications, palmitoylation, and alternative Cys-based redox modifications. In this minireview, we discuss the mechanisms through which S-nitrosylation exerts its broad pleiotropic influence on protein post-translational modification.

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Figures

FIGURE 1.
FIGURE 1.
Schematic summary of principal post-translational mechanisms regulated by S-nitrosylation and molecular loci of regulation.
See this image and copyright information in PMC

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