Activation State - Dependent Interaction between G i and p 67 phox
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چکیده
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 i subunit of heterotrimeric G proteins is a novel binding partner for p67 in transfected HEK293T cells and peripheral blood polymorphonuclear leukocytes. p67 preferably interacted with inactive G i. Expression of p67 caused a dose-dependent decrease in intracellular cyclic AMP concentration, suggesting altered function of G i. We identified a fragment of p67, consisting of the PB1 domain and the C-terminal SH3 domain, to be critical for the interaction with G i. Because these domains are involved in the interaction with p47 and p40, the relationship between the respective binding events was investigated. Wild-type G i, but not its QL mutant, could promote the interaction between p67 and p47. However, the interaction between p67 and p40 was not affected by either G i form. These results provide the first evidence for an interaction between p67 and an alpha subunit of heterotrimeric G proteins, suggesting a potential role for G i in the regulation or activation of NADPH oxidase.
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تاریخ انتشار 2005