Gp91
            <i>
              <sup>phox</sup>
            </i>
            is the heme binding subunit of the superoxide-generating NADPH oxidase

Yu, Liping; Quinn, Mark T.; Cross, Andrew R.; Dinauer, Mary C.

doi:10.1073/pnas.95.14.7993

Cited by 198 publications

(171 citation statements)

References 44 publications

(47 reference statements)

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“…The deduced sequences contain conserved features considered critical for NADPH oxidase function (1), namely six hydrophobic segments within the N-terminal segment, proposed as membrane-embedded domains involved in transmembrane electron transport, as well as sequence motifs corresponding to proposed binding sites for heme, flavin, and NADPH. The third and fifth hydrophobic segments each contain two conserved histidines, which are thought to serve as coordination sites for two heme moieties within the corresponding sequences of gp91 phox and ferric reductase (13,14). Other sites exhibiting high homology occur within the C-terminal portion, corresponding to gp91 phox sequences that are thought to represent binding sites for flavin and NADPH (Fig.…”

Section: Resultsmentioning

confidence: 99%

Identification of Renox, an NAD(P)H oxidase in kidney

Geiszt

Kopp

Várnai

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

766

612

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Oxygen sensing is essential for homeostasis in all aerobic organisms, but its mechanism is poorly understood. Data suggest that a phagocytic-like NAD(P)H oxidase producing reactive oxygen species serves as a primary sensor for oxygen. We have characterized a source of superoxide anions in the kidney that we refer to as a renal NAD(P)H oxidase or Renox. Renox is homologous to gp91 phox (91-kDa subunit of the phagocyte oxidase), the electron-transporting subunit of phagocytic NADPH oxidase, and contains all of the structural motifs considered essential for binding of heme, flavin, and nucleotide. In situ RNA hybridization revealed that renox is highly expressed at the site of erythropoietin production in the renal cortex, showing the greatest accumulation of renox mRNA in proximal convoluted tubule epithelial cells. NIH 3T3 fibroblasts overexpressing transfected Renox show increased production of superoxide and develop signs of cellular senescence. Our data suggest that Renox, as a renal source of reactive oxygen species, is a likely candidate for the oxygen sensor function regulating oxygen-dependent gene expression and may also have a role in the development of inflammatory processes in the kidney.

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Section: Resultsmentioning

confidence: 99%

Identification of Renox, an NAD(P)H oxidase in kidney

Geiszt

Kopp

Várnai

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

766

612

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“…Previously, it has been extensively demonstrated that the interaction of p22phox with Nox2 is required to form a functionally active enzyme in leukocytes (5). Recently, it was also demonstrated that co-transfection of p22phox together with Nox1 is required to facilitate Nox1-mediated O 2 Ϫ generation in CHO-cells, which reportedly lack endogenous p22phox expression (16).…”

Section: Discussionmentioning

confidence: 99%

“…The anchoring of the hemes in the cytochrome b 558 occurs via four histidines located at positions 101, 115, 209, and 222 in Nox2 (5). Mutation of any of these histidines, resulting in the loss of a heme in Nox2, leads to a conformational change in the protein and not only prevents O 2 Ϫ formation but also disrupts the interaction of Nox2 with p22phox (6).…”

mentioning

confidence: 99%

Direct Interaction of the Novel Nox Proteins with p22phox Is Required for the Formation of a Functionally Active NADPH Oxidase

Ambasta

Kumar

Griendling

et al. 2004

Journal of Biological Chemistry

477

376

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Nox1 and Nox4, homologues of the leukocyte NADPH oxidase subunit Nox2 (gp91phox) mediate superoxide anion formation in various cell types. However, their interactions with other components of the NADPH oxidase are poorly defined. We determined whether a direct interaction of Nox1 and Nox4 with the p22phox subunit of the NADPH oxidase occurs. Using confocal microscopy, co-localization of p22phox with Nox1, Nox2, and Nox4 was observed in transiently transfected vascular smooth muscle cells (VSMC) and HEK293 cells. Plasmids coding for fluorescent fusion proteins of p22phox and the Nox proteins with cyan-and yellowfluorescent protein (cfp and yfp, respectively) were constructed and expressed in VSMC and HEK293 cells. The cfp-tagged p22phox expression level increased upon cotransfection with Nox1 or Nox4. Protein-protein interaction between the fluorescent fusion proteins of p22phox and the Nox partners was observed using the fluorescence resonance energy transfer technique. Immunoprecipitation of native Nox1 from human VSMC revealed co-precipitation of p22phox. Immunoprecipitation from transfected HEK293 cells revealed co-precipitation of native p22phox with yfp-tagged Nox1, Nox2, and Nox4. Following mutation of a histidine (corresponding to the position 115 in human Nox2) to leucine, this interaction was abolished. Transfection of rat p22phox (but not Noxo1 and Noxa1) increased the radical generation in cells expressing Nox4. We provide evidence that p22phox directly interacts with Nox1 and Nox4, to form an superoxide-generating NADPH oxidase and demonstrate that mutation of the potential heme binding site in the Nox proteins disrupts the complex formation of Nox1 and Nox4 with p22phox.

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“…Although the topology and functions of plant rboh proteins have not been tested experimentally, several features of the amino acid sequence and comparisons with human gp91 phox allow predictions (Yu et al, 1998). NbrbohA and NbrbohB proteins are predicted to have six transmembrane-spanning domains (TMD-1 to TMD-6) that correspond to those identified in gp91 phox .…”

Section: Two Cdnas For the Gp91 Phox Homolog In N Benthamianamentioning

confidence: 99%

Nicotiana benthamiana gp91^phox Homologs NbrbohA and NbrbohB Participate in H₂O₂ Accumulation and Resistance to Phytophthora infestans

et al. 2003

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Active oxygen species (AOS) are responsible for triggering defense responses in plants. Respiratory burst oxidase homologs ( rboh genes) have been implicated in AOS generation. We have isolated two rboh cDNAs, NbrbohA and NbrbohB , from Nicotiana benthamiana leaves. NbrbohA was expressed constitutively at a low level and the transcripts were increased after mechanical stress of control leaf infiltration, whereas NbrbohB was induced specifically by the protein elicitor INF1 from the potato pathogen Phytophthora infestans . We examined the function of the Nbrboh genes in AOS generation and in the hypersensitive response (HR) using virus-induced gene silencing (VIGS). VIGS indicated that both genes are required for H 2 O 2 accumulation and for resistance to Phytophthora. VIGS of Nbrboh genes also led to a reduction and delay of HR cell death caused by INF1. We further demonstrate that the induction of HR-like cell death by overexpression of a constitutively active mutant of a mitogen-activated protein kinase kinase, MEK DD , is compromised by VIGS of NbrbohB . We found that MEK DD induced NbrbohB but not NbrbohA . This work provides genetic evidence for the involvement of a mitogen-activated protein kinase cascade in the regulation of rboh genes.

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Gp91 ^phox is the heme binding subunit of the superoxide-generating NADPH oxidase

Abstract: The

Cited by 198 publications

References 44 publications

Identification of Renox, an NAD(P)H oxidase in kidney

Identification of Renox, an NAD(P)H oxidase in kidney

Direct Interaction of the Novel Nox Proteins with p22phox Is Required for the Formation of a Functionally Active NADPH Oxidase

Nicotiana benthamiana gp91^phox Homologs NbrbohA and NbrbohB Participate in H₂O₂ Accumulation and Resistance to Phytophthora infestans

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Gp91 phox is the heme binding subunit of the superoxide-generating NADPH oxidase

Abstract: The

Cited by 198 publications

References 44 publications

Identification of Renox, an NAD(P)H oxidase in kidney

Identification of Renox, an NAD(P)H oxidase in kidney

Direct Interaction of the Novel Nox Proteins with p22phox Is Required for the Formation of a Functionally Active NADPH Oxidase

Nicotiana benthamiana gp91phox Homologs NbrbohA and NbrbohB Participate in H2O2 Accumulation and Resistance to Phytophthora infestans

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Gp91 ^phox is the heme binding subunit of the superoxide-generating NADPH oxidase

Nicotiana benthamiana gp91^phox Homologs NbrbohA and NbrbohB Participate in H₂O₂ Accumulation and Resistance to Phytophthora infestans