Unraveling the S-nitrosoproteome: tools and strategies.
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.
López-Sánchez
Laura M
LM
Unidad de Investigación, Hospital Universitario Reina Sofía, Córdoba, Spain.
Muntané
Jordi
J
de la Mata
Manuel
M
Rodríguez-Ariza
Antonio
A
D000818:Animals; D001710:Biotin / Q000378:metabolism; D002450:Cell Communication; D003545:Cysteine / Q000378:metabolism; D006801:Humans; D051379:Mice; D009569:Nitric Oxide / Q000378:metabolism; D015538:Nitrosation; D010084:Oxidation-Reduction; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D051381:Rats; D026403:S-Nitrosothiols / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000378:metabolism
D011506:Proteins; D026403:S-Nitrosothiols; D013438:Sulfhydryl Compounds; D009569:Nitric Oxide; D001710:Biotin; D003545:Cysteine