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	Biochem. Biophys. Res. Commun. Nov (2001); 289(2):382-8
The NADPH oxidase components p47(phox) and p40(phox) bind to moesin through their PX domain.
Wientjes FB, Reeves EP, Soskic V, Furthmayr H, Segal AW
Centre for Molecular Medicine, University College London, 5 University Street, London WC1E 6JJ, United Kingdom. rmhafrw@ucl.ac.uk
Abstract: The NADPH oxidase of phagocytes is a membrane-bound heterodimeric flavocytochrome which catalyses the transfer of electrons from NADPH in the cytoplasm to oxygen in the phagosome. A number of cytosolic proteins are involved in its activation/deactivation: p47phox, p67phox, p40phox and the small GTP-binding protein, rac. The cytosolic phox proteins interact with the cytoskeleton in human neutrophils and, in particular, an interaction with coronin has been reported (Grogan A., Reeves, E., Keep, N. H., Wientjes, F., Totty, N., Burlingame, N. L., Hsuan, J., and Segal, A. W. (1997) J. Cell Sci. 110, 3071-3081). Here, we report on the interaction of another cytoskeletal protein, moesin, with the phox proteins. Moesin belongs to the ezrin-radixin-moesin family of F-actin-binding proteins and we show that it binds to p47phox and p40phox in a phosphoinositide-dependent manner. Furthermore, we show that its N-terminal part binds to the PX domain of p47phox and p40phox.
[PUBMED: 11716484]