Mechanism for interaction between gp91phox and p22phox : two membrane-integrated proteins of the phagocyte NADPH oxidase

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The phagocyte NADPH oxidase, dormant in resting cells, is activated during phagocytosis to produce superoxide, a precursor of microbicidal oxidants. The catalytic core of the phagocyte oxidase is Nox2/gp91^<phox>, a membrane-spaning protein that forms a stable heterodimer with p22^<phox>. In this study, I found that both N- and C-terminal regions play a crucial role in Nox binding to p22^<phox>. Furthermore, I showed that a short region between the TPR and activation domains in p67^<phox> is crucial for activation of Nox2.