Purification of reversibly oxidized proteins (PROP) reveals a redox switch controlling p38 MAP kinase activity.

ABSTRACT: Oxidation of cysteine residues of proteins is emerging as an important means of regulation of signal transduction, particularly of protein kinase function. Tools to detect and quantify cysteine oxidation of proteins have been a limiting factor in understanding the role of cysteine oxidation in signal transduction. As an example, the p38 MAP kinase is activated by several stress-related stimuli that are often accompanied by in vitro generation of hydrogen peroxide. We noted that hydrogen peroxide inhibited p38 activity despite paradoxically increasing the activating phosphorylation of p38. To address the possibility that cysteine oxidation may provide a negative regulatory effect on p38 activity, we developed a biochemical assay to detect reversible cysteine oxidation in intact cells. This

SUBMITTER: Templeton DJ 

PROVIDER: S-EPMC2981573 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature