Regulation of protein function and signaling by reversible cysteine S-nitrosylation

J Biol Chem. 2013 Sep 13;288(37):26473-9. doi: 10.1074/jbc.R113.460261. Epub 2013 Jul 16.

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.

Keywords: Nitric Oxide; Nitric-oxide Synthase; Nitrosylation; Post-translational Modification; Protein Chemistry; Proteomics; S-Nitrosocysteine; S-Nitrosothiols.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Cysteine / analogs & derivatives*
  • Cysteine / chemistry
  • Gene Expression Regulation*
  • Humans
  • Mice
  • Myocardium / metabolism
  • Nitric Oxide / chemistry
  • Nitric Oxide Synthase / metabolism
  • Nitrogen / chemistry
  • Oxidation-Reduction
  • Protein Processing, Post-Translational
  • Proteins / chemistry*
  • Proteomics / methods
  • S-Nitrosothiols / chemistry*
  • Signal Transduction

Substances

  • Proteins
  • S-Nitrosothiols
  • Nitric Oxide
  • S-nitrosocysteine
  • Nitric Oxide Synthase
  • Cysteine
  • Nitrogen