Regulation of the phagocyte NADPH oxidase activity: phosphorylation of gp91phox/NOX2 by protein kinase C enhances its diaphorase activity and binding to Rac2, p67phox, and p47phox.

@article{Raad2009RegulationOT,
  title={Regulation of the phagocyte NADPH oxidase activity: phosphorylation of gp91phox/NOX2 by protein kinase C enhances its diaphorase activity and binding to Rac2, p67phox, and p47phox.},
  author={Houssam Raad and M H Paclet and Tarek Boussetta and Yolande Kroviarski and Françoise Morel and Mark T Quinn and Marie-Anne Gougerot-Pocidalo and Pham My-Chan Dang and Jamel El-Benna},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2009},
  volume={23 4},
  pages={1011-22}
}
Neutrophils generate microbicidal oxidants through activation of a multicomponent enzyme called NADPH oxidase. During activation, the cytosolic NADPH oxidase components (p47(phox), p67(phox), p40(phox), and Rac2) translocate to the membranes, where they associate with flavocytochrome b(558), which is composed of gp91(phox)/NOX2 and p22(phox), to form the active system. During neutrophil stimulation, p47(phox), p67(phox), p40(phox), and p22(phox) are phosphorylated; however, the phosphorylation… CONTINUE READING