Unraveling the S-nitrosoproteome: tools and strategies

Proteomics. 2009 Feb;9(4):808-18. doi: 10.1002/pmic.200800546.

Abstract

One of the major tasks to be accomplished in the postgenomic era is the characterization of PTMs in proteins. The S-nitrosation of protein thiols is a redox-based PTM that modulating enzymatic activity, subcellular localization, complex formation, and degradation of proteins, largely contributes to the complexity of cellular proteomes. Although the detection of S-nitrosated proteins is problematical due to the lability of S-nitrosothiols, with the improvement of molecular tools an increasing range of proteins has been shown to undergo S-nitrosation. We here review recent proteomic approaches for the systematic assessment of potential targets for protein S-nitrosation. The development of new analytical methods and strategies over the past several years now allows us to investigate the nitrosoproteome on a global scale.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Biotin / metabolism
  • Cell Communication
  • Cysteine / metabolism
  • Humans
  • Mice
  • Nitric Oxide / metabolism
  • Nitrosation*
  • Oxidation-Reduction
  • Protein Processing, Post-Translational*
  • Proteins / metabolism*
  • Proteomics / methods*
  • Rats
  • S-Nitrosothiols / metabolism*
  • Sulfhydryl Compounds / metabolism

Substances

  • Proteins
  • S-Nitrosothiols
  • Sulfhydryl Compounds
  • Nitric Oxide
  • Biotin
  • Cysteine