Work

Regulation by S-Nitrosylation of Protein Post-translational Modification

Year: 2011

Type: review

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.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.r111.285742

Authors: Douglas T. Hess, Jonathan S. Stamler

Institutions: Case Western Reserve University, University Hospitals of Cleveland, University Hospitals Cleveland Medical Center

Language: English

Topic: Redox biology and oxidative stress

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funder: National Heart, Lung, and Blood Institute