Methionine residues around phosphorylation sites are preferentially oxidized in vivo under stress conditions.

ABSTRACT: Protein phosphorylation is one of the most prevalent and well-understood protein modifications. Oxidation of protein-bound methionine, which has been traditionally perceived as an inevitable damage derived from oxidative stress, is now emerging as another modification capable of regulating protein activity during stress conditions. However, the mechanism coupling oxidative signals to changes in protein function remains unknown. An appealing hypothesis is that methionine oxidation might serve as a rheostat to control phosphorylation. To investigate this potential crosstalk between phosphorylation and methionine oxidation, we have addressed the co-occurrence of these two types of modifications within the human proteome. Here, we show that nearly all (98%) proteins containing oxidized methion

SUBMITTER: Veredas FJ 

PROVIDER: S-EPMC5227694 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature