Cited by 380Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressNitric Oxide and Endothelin Effects

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Novel Human Homologues of p47 and p67 Participate in Activation of Superoxide-producing NADPH Oxidases

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Takeya, Ryu, Ueno, Noriko, Kami, Keiichiro, Taura, Masahiko, Kohjima, Motoyuki, Izaki, Tomoko, Nunoi, Hiroyuki, Sumimoto, Hideki·2003·Journal of Biological Chemistry

DOI 10.1074/jbc.m212856200PMC PMC4358237

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Abstract

The catalytic core of a superoxide-producing NADPH oxidase (Nox) in phagocytes is gp91phox/Nox2, a membrane-integrated protein that forms a heterodimer with p22phox to constitute flavocytochrome b558. The cytochrome becomes activated by interacting with the adaptor proteins p47phox and p67phox as well as the small GTPase Rac. Here we describe the cloning of human cDNAs for novel proteins homologous to p47phox and p67phox, designated p41nox and p51nox, respectively; the former is encoded by NOXO1 (Nox organizer 1), and the latter is encoded by NOXA1 (Nox activator 1). The novel homologue p41nox interacts with p22phox via the two tandem SH3 domains, as does p47phox. The protein p51nox as well as p67phox can form a complex with p47phox and with p41nox via the C-terminal SH3 domain and binds to GTP-bound Rac via the N-terminal domain containing four tetratricopeptide repeat motifs. These bindings seem to play important roles, since p47phox and p67phox activate the phagocyte oxidase via the same interactions. Indeed, p41nox and p51nox are capable of replacing the corresponding classical homologue in activation of gp91phox. Nox1, a homologue of gp91phox, also can be activated in cells, when it is coexpressed with p41nox and p51nox, with p41nox and p67phox, or with p47phox and p51nox; in the former two cases, Nox1 is partially activated without any stimulants added, suggesting that p41nox is normally in an active state. Thus, the novel homologues p41nox and p51nox likely function together or in combination with a classical one, thereby activating the two Nox family oxidases.

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Authors: Takeya, R., Ueno, N., Kami, K., Taura, M., Kohjima, M., Izaki, T., Nunoi, H., & Sumimoto, H.
Affiliations: Kyushu University (JP)
University of Miyazaki (JP)
Corresponding author: Sumimoto, Hideki
ORCID: Takeya, Ryu
Kohjima, Motoyuki
Nunoi, Hiroyuki
Sumimoto, Hideki
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2003-07
Volume: 278
Issue: 27
Pages: 25234-25246
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m212856200
PMC: PMC4358237
OpenAlex: W2003241255
Cited by: 380
References: 58
Citations by year: 2026: 3 · 2025: 6 · 2024: 3 · 2023: 10 · 2022: 5 · 2021: 8 · 2020: 9 · 2019: 11 · 2018: 7 · 2017: 14 · 2016: 9 · 2015: 9 · 2014: 13 · 2013: 20 · 2012: 15
FWCI: 12.69
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6305 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
Keywords: NADPH oxidase, p47phox, p67phox, NOXO1, NOXA1, gp91phox, p22phox, flavocytochrome b558, Rac GTPase, SH3 domain, NOX1, superoxide production, phagocytes, oxidase activation, adaptor proteins
MeSH terms: Amino Acid Sequence, Cloning, Molecular, Enzyme Activation, Humans, Molecular Sequence Data, Phosphoproteins, Genome, Human, Sequence Alignment, Sequence Homology, DNA, Complementary, NADPH Oxidases, Adaptor Proteins, Vesicular Transport, Adaptor Proteins, Signal Transducing

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Novel Human Homologues of p47 and p67 Participate in Activation of Superoxide-producing NADPH Oxidases

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