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JEM © The Rockefeller University Press $8.00 Vol. 203, No. 8, August 7, 2006 1915–1925 www.jem.org/cgi/doi/10.1084/jem.20052085 1915 Phagocytic leukocytes are essential for intact innate immunity to bacterial and fungal pathogens. Upon activation by either soluble stimuli or during phagocytosis, a reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidase generates large quantities of superoxide at the plasma or phagosomal membrane, which is converted into reactive oxidants used for microbial killing (1–3). The phagocyte NADPH oxidase is comprised of two integral membrane proteins, gp91phox and p22phox, that together form the oxidase fl avocytochrome b558, as well as p47phox, p67phox, and Rac-GTP, which translocate from the cytosol to the membrane to activate electron transport through the fl avocytochrome (2, 3). Attesting to its importance in host defense, genetic defects in the aforementioned phox (phagocyte oxidase) subunits result in chronic granulomatous disease, an inherited disorder characterized by recurrent pyogenic infections (1). Conversely, excessive or inappropriate superoxide release has been implicated in the pathogenesis of infl ammatory tissue injury. Hence, the activity of this enzyme is highly regulated. NADPH oxidase activation is triggered by still incompletely defi ned events downstream of cell surface receptors engaged by opsonized microbes or soluble infl ammatory mediators. These include phosphorylation of p47phox on multiple serine residues, which unmasks tandem SH3 domains that bind to a proline-rich motif The phosphoinositide-binding protein p40phox activates the NADPH oxidase during FcγΙΙΑ receptor–induced phagocytosis

The phosphoinositide-binding protein p40phox activates the NADPH oxidase during FcγIIA receptor–induced phagocytosis