p40phox as an alternative organizer to p47phox in Nox2 activation: A new mechanism involving an interaction with p22phox

Minoru Tamura; Iichiro Shiozaki; Shohei Ono; Kei Miyano; Sachio Kunihiro; Takayuki Sasaki

doi:10.1016/j.febslet.2007.08.040

p40^phox as an alternative organizer to p47^phox in Nox2 activation: A new mechanism involving an interaction with p22^phox

Minoru Tamura, Iichiro Shiozaki, Shohei Ono, Kei Miyano, Sachio Kunihiro, Takayuki Sasaki

Center for Cohort Studies

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

11 Citations (Scopus)

Abstract

p40^phox activated phagocyte NADPH oxidase without p47^phox in a cell-free system consisting of p67^phox, Rac and cytochrome b₅₅₈ relipidated with phosphatidylinositol 3-phosphate. The activation reached to 70% of that by p47^phox. Addition of p47^phox slightly increased the activation, but not additively. p40^phox improved the efficiency of p67^phox in the activation. The C-terminus-truncated p67^phox, p40^phox(D289A), p40^phox(R58A), or p40^phox(W207R) showed an impaired activation. A peptide corresponding to the p22^phox Pro-rich region suppressed the activation, and far-western blotting revealed its interaction with p40^phox SH3 domain. Thus, p40^phox can substitute for p47^phox in the activation, interacting with p22^phox and p67^phox through their specific regions.

Original language	English
Pages (from-to)	4533-4538
Number of pages	6
Journal	FEBS Letters
Volume	581
Issue number	23
DOIs	https://doi.org/10.1016/j.febslet.2007.08.040
Publication status	Published - Sep 18 2007

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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@article{3da7d9fc6db549cbadc476de2b3a5a9f,

title = "p40phox as an alternative organizer to p47phox in Nox2 activation: A new mechanism involving an interaction with p22phox",

abstract = "p40phox activated phagocyte NADPH oxidase without p47phox in a cell-free system consisting of p67phox, Rac and cytochrome b558 relipidated with phosphatidylinositol 3-phosphate. The activation reached to 70% of that by p47phox. Addition of p47phox slightly increased the activation, but not additively. p40phox improved the efficiency of p67phox in the activation. The C-terminus-truncated p67phox, p40phox(D289A), p40phox(R58A), or p40phox(W207R) showed an impaired activation. A peptide corresponding to the p22phox Pro-rich region suppressed the activation, and far-western blotting revealed its interaction with p40phox SH3 domain. Thus, p40phox can substitute for p47phox in the activation, interacting with p22phox and p67phox through their specific regions.",

author = "Minoru Tamura and Iichiro Shiozaki and Shohei Ono and Kei Miyano and Sachio Kunihiro and Takayuki Sasaki",

year = "2007",

month = sep,

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doi = "10.1016/j.febslet.2007.08.040",

language = "English",

volume = "581",

pages = "4533--4538",

journal = "FEBS Letters",

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T1 - p40phox as an alternative organizer to p47phox in Nox2 activation

T2 - A new mechanism involving an interaction with p22phox

AU - Tamura, Minoru

AU - Shiozaki, Iichiro

AU - Ono, Shohei

AU - Miyano, Kei

AU - Kunihiro, Sachio

AU - Sasaki, Takayuki

PY - 2007/9/18

Y1 - 2007/9/18

N2 - p40phox activated phagocyte NADPH oxidase without p47phox in a cell-free system consisting of p67phox, Rac and cytochrome b558 relipidated with phosphatidylinositol 3-phosphate. The activation reached to 70% of that by p47phox. Addition of p47phox slightly increased the activation, but not additively. p40phox improved the efficiency of p67phox in the activation. The C-terminus-truncated p67phox, p40phox(D289A), p40phox(R58A), or p40phox(W207R) showed an impaired activation. A peptide corresponding to the p22phox Pro-rich region suppressed the activation, and far-western blotting revealed its interaction with p40phox SH3 domain. Thus, p40phox can substitute for p47phox in the activation, interacting with p22phox and p67phox through their specific regions.

AB - p40phox activated phagocyte NADPH oxidase without p47phox in a cell-free system consisting of p67phox, Rac and cytochrome b558 relipidated with phosphatidylinositol 3-phosphate. The activation reached to 70% of that by p47phox. Addition of p47phox slightly increased the activation, but not additively. p40phox improved the efficiency of p67phox in the activation. The C-terminus-truncated p67phox, p40phox(D289A), p40phox(R58A), or p40phox(W207R) showed an impaired activation. A peptide corresponding to the p22phox Pro-rich region suppressed the activation, and far-western blotting revealed its interaction with p40phox SH3 domain. Thus, p40phox can substitute for p47phox in the activation, interacting with p22phox and p67phox through their specific regions.

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