Protein tyrosine nitration: a signaling mechanism conserved from yeast to man

Although protein nitration had already been reported in the late forties and found to specifically affect tyrosine residues 20 years later, it was not until the early nineties that this post-translational modification was reported to occur in vivo in mammalian cells. Over the years, this protein modification has increasingly proven to play a major role in a variety of physiological mechanisms through redox signaling and pathological conditions through nitro-oxidative stress, from protozoan parasites to humans. In this issue (Proteomics 2015, 15, 580-590), Kang et al. report the identification of the nitroproteome during mating in the yeast Saccharomyces cerevisiae and most interestingly on the changes in nitration induced by the mating signal α-factor of several of these proteins. The correlation of these modifications with the biological functions of these proteins strongly suggests a role for protein nitration in mating signal transduction in yeast, thereby confirming the conservation of this pathway throughout the evolution from unicellular eukaryotes to man. The ubiquity of protein tyrosine nitration, whose importance is now also recognized in plants, further highlights its significance as an essential signaling mechanism in eukaryotes.