Title: Regulation of protein function and signaling by reversible cysteine S-nitrosylation.
Authors: Gould, Neal; Doulias, Paschalis-Thomas; Tenopoulou, Margarita; Raju, Karthik; Ischiropoulos, Harry
Published In J Biol Chem, (2013 Sep 13)
Abstract: NO is a versatile free radical that mediates numerous biological functions within every major organ system. A molecular pathway by which NO accomplishes functional diversity is the selective modification of protein cysteine residues to form S-nitrosocysteine. This post-translational modification, S-nitrosylation, impacts protein function, stability, and location. Despite considerable advances with individual proteins, the in vivo biological chemistry, the structural elements that govern the selective S-nitrosylation of cysteine residues, and the potential overlap with other redox modifications are unknown. In this minireview, we explore the functional features of S-nitrosylation at the proteome level and the structural diversity of endogenously modified residues, and we discuss the potential overlap and complementation that may exist with other cysteine modifications.
PubMed ID: 23861393
MeSH Terms: Animals; Cysteine/analogs & derivatives*; Cysteine/chemistry; Gene Expression Regulation*; Humans; Mice; Myocardium/metabolism; Nitric Oxide Synthase/metabolism; Nitric Oxide/chemistry; Nitrogen/chemistry; Oxidation-Reduction; Protein Processing, Post-Translational; Proteins/chemistry*; Proteomics/methods; S-Nitrosothiols/chemistry*; Signal Transduction