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Molecular and Cellular Biology, July 2006, p. 5190-5200, Vol. 26, No. 13
0270-7306/06/$08.00+0     doi:10.1128/MCB.01979-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Activation State-Dependent Interaction between G{alpha}i and p67phox

Caroline Marty,1 Tohru Kozasa,1 Mark T. Quinn,2 and Richard D. Ye1*

Department of Pharmacology, College of Medicine, University of Illinois, Chicago, Illinois 60612,1 Department of Veterinary Molecular Biology, Montana State University, Bozeman, Montana 597172

Received 10 October 2005/ Returned for modification 3 November 2005/ Accepted 13 April 2006

The phagocyte NADPH oxidase consists of multiple protein subunits that interact with each other to form a functional superoxide-generating complex. Although the essential components for superoxide production have been well characterized, other proteins potentially involved in the regulation of NADPH oxidase activation remain to be identified. We report here that the G{alpha}i subunit of heterotrimeric G proteins is a novel binding partner for p67phox in transfected HEK293T cells and peripheral blood polymorphonuclear leukocytes. p67phox preferably interacted with inactive G{alpha}i. Expression of p67phox caused a dose-dependent decrease in intracellular cyclic AMP concentration, suggesting altered function of G{alpha}i. We identified a fragment of p67phox, consisting of the PB1 domain and the C-terminal SH3 domain, to be critical for the interaction with G{alpha}i. Because these domains are involved in the interaction with p47phox and p40phox, the relationship between the respective binding events was investigated. Wild-type G{alpha}i, but not its QL mutant, could promote the interaction between p67phox and p47phox. However, the interaction between p67phox and p40phox was not affected by either G{alpha}i form. These results provide the first evidence for an interaction between p67phox and an alpha subunit of heterotrimeric G proteins, suggesting a potential role for G{alpha}i in the regulation or activation of NADPH oxidase.

* Corresponding author. Mailing address: Department of Pharmacology, University of Illinois at Chicago, 835 S. Wolcott Avenue, Chicago, IL 60612. Phone: (312) 996-5087. Fax: (312) 996-7857. E-mail: yer{at}uic.edu.

Molecular and Cellular Biology, July 2006, p. 5190-5200, Vol. 26, No. 13
0270-7306/06/$08.00+0     doi:10.1128/MCB.01979-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.





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