Phosphorylation of p22phox on threonine 147 enhances NADPH oxidase activity by promoting p47phox binding.

The Journal of Biological Chemistry
Eric M LewisLinda C McPhail

Abstract

NADPH oxidase comprises both cytosolic and membrane-bound subunits, which, when assembled and activated, initiate the transfer of electrons from NADPH to molecular oxygen to form superoxide. This activity, known as the respiratory burst, is extremely important in the innate immune response as indicated by the disorder chronic granulomatous disease. The regulation of this enzyme complex involves protein-protein and protein-lipid interactions as well as phosphorylation events. Previously, our laboratory demonstrated that the small membrane subunit of the oxidase complex, p22(phox), is phosphorylated in neutrophils and that its phosphorylation correlates with NADPH oxidase activity. In this study, we utilized site-directed mutagenesis in a Chinese hamster ovarian cell system to determine the phosphorylation sites within p22(phox). We also explored the mechanism by which p22(phox) phosphorylation affects NADPH oxidase activity. We found that mutation of threonine 147 to alanine inhibited superoxide production in vivo by more than 70%. This mutation also blocked phosphorylation of p22(phox) in vitro by both protein kinase C-alpha and -delta. Moreover, this mutation blocked the p22(phox)-p47(phox) interaction in intact cells. When ph...Continue Reading

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