Molecular interaction of NADPH oxidase 1 with betaPix and Nox Organizer 1.

It is well established that growth-factor-induced reactive oxygen species (ROS) act as second messengers in cell signaling. We have previously reported that betaPix, a guanine nucleotide exchange factor for Rac, interacts with NADPH oxidase 1 (Nox1) leading to EGF-induced ROS generation. Here, we report the identification of the domains of ...
Nox1 and betaPix responsible for the interaction between the two proteins. GST pull-down assays show that the PH domain of betaPix binds to the FAD-binding region of Nox1. We also show that overexpression of the PH domain of betaPix results in inhibition of superoxide anion generation in response to EGF. Additionally, NADPH oxidase Organizer 1 (NoxO1) is shown to interact with the NADPH-binding region of Nox1. These results suggest that the formation of the complex consisting of Nox1, betaPix, and NoxO1 is likely to be a critical step in EGF-induced ROS generation.
Mesh Terms:
Adaptor Proteins, Vesicular Transport, Cell Cycle Proteins, Cell Line, Epidermal Growth Factor, Guanine Nucleotide Exchange Factors, Humans, Kidney, NADPH Oxidase 1, NADPH Oxidases, Protein Binding, Reactive Oxygen Species, Recombinant Proteins, Rho Guanine Nucleotide Exchange Factors, Superoxides
Biochem. Biophys. Res. Commun.
Date: Jan. 20, 2006
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