Molecular interaction of NADPH oxidase 1 with βpix and Nox Organizer 1

Hye Sun Park; Dongeun Park; Yun Soo Bae

doi:10.1016/j.bbrc.2005.11.108

Molecular interaction of NADPH oxidase 1 with βpix and Nox Organizer 1

Hye Sun Park, Dongeun Park, Yun Soo Bae

Department of Life Science

Research output: Contribution to journal › Article › peer-review

26 Scopus citations

Abstract

It is well established that growth-factor-induced reactive oxygen species (ROS) act as second messengers in cell signaling. We have previously reported that βPix, 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 βPix responsible for the interaction between the two proteins. GST pull-down assays show that the PH domain of βPix binds to the FAD-binding region of Nox1. We also show that overexpression of the PH domain of βPix 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, βPix, and NoxO1 is likely to be a critical step in EGF-induced ROS generation.

Original language	English
Pages (from-to)	985-990
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	339
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2005.11.108
State	Published - 20 Jan 2006

Bibliographical note

Funding Information:
We thank Dr. Sumimoto for the plasmid DNA (pEF-Bos-NoxO1 and pEF-Bos-NoxA1) and Dr. Leto for the retrovirus encoding Nox1. We thank Dr. Jaesang Kim for critical reading. This work is supported by the Korea Science and Engineering Foundation (KOSEF) through the Center for Cell Signaling Research at Ewha Womans University, by 21st Century Frontier Functional Proteomics Project (FPR05C2-510), and by Grant M103KV010013-04K2201-01310 to D.P. from Brain Research Center of the 21st Century Frontier Research Program from the Ministry of Science and Technology. H.S.P. is the recipient of BK21 scholarship and of KRF-2005-216-C00126 from Korea Research Foundation.

Keywords

EGF
NADPH oxidase 1
NADPH oxidase Organizer 1
Reactive oxygen species
Superoxide anion
βPix

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10.1016/j.bbrc.2005.11.108

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title = "Molecular interaction of NADPH oxidase 1 with βpix and Nox Organizer 1",

abstract = "It is well established that growth-factor-induced reactive oxygen species (ROS) act as second messengers in cell signaling. We have previously reported that βPix, 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 βPix responsible for the interaction between the two proteins. GST pull-down assays show that the PH domain of βPix binds to the FAD-binding region of Nox1. We also show that overexpression of the PH domain of βPix 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, βPix, and NoxO1 is likely to be a critical step in EGF-induced ROS generation.",

keywords = "EGF, NADPH oxidase 1, NADPH oxidase Organizer 1, Reactive oxygen species, Superoxide anion, βPix",

author = "Park, {Hye Sun} and Dongeun Park and Bae, {Yun Soo}",

note = "Funding Information: We thank Dr. Sumimoto for the plasmid DNA (pEF-Bos-NoxO1 and pEF-Bos-NoxA1) and Dr. Leto for the retrovirus encoding Nox1. We thank Dr. Jaesang Kim for critical reading. This work is supported by the Korea Science and Engineering Foundation (KOSEF) through the Center for Cell Signaling Research at Ewha Womans University, by 21st Century Frontier Functional Proteomics Project (FPR05C2-510), and by Grant M103KV010013-04K2201-01310 to D.P. from Brain Research Center of the 21st Century Frontier Research Program from the Ministry of Science and Technology. H.S.P. is the recipient of BK21 scholarship and of KRF-2005-216-C00126 from Korea Research Foundation.",

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N2 - It is well established that growth-factor-induced reactive oxygen species (ROS) act as second messengers in cell signaling. We have previously reported that βPix, 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 βPix responsible for the interaction between the two proteins. GST pull-down assays show that the PH domain of βPix binds to the FAD-binding region of Nox1. We also show that overexpression of the PH domain of βPix 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, βPix, and NoxO1 is likely to be a critical step in EGF-induced ROS generation.

AB - It is well established that growth-factor-induced reactive oxygen species (ROS) act as second messengers in cell signaling. We have previously reported that βPix, 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 βPix responsible for the interaction between the two proteins. GST pull-down assays show that the PH domain of βPix binds to the FAD-binding region of Nox1. We also show that overexpression of the PH domain of βPix 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, βPix, and NoxO1 is likely to be a critical step in EGF-induced ROS generation.

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Molecular interaction of NADPH oxidase 1 with βpix and Nox Organizer 1

Abstract

Bibliographical note

Keywords

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