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Volumn 93, Issue 3, 2013, Pages 427-435

Identification of a region in p47phox/NCF1 crucial for phagocytic NADPH oxidase (NOX2) activation

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; MUTANT PROTEIN; P47PHOX PROTEIN; PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; TYRAMINE; UNCLASSIFIED DRUG; VALINE;

EID: 84874542636     PISSN: 07415400     EISSN: 19383673     Source Type: Journal    
DOI: 10.1189/jlb.1211588     Document Type: Article
Times cited : (49)

References (40)
  • 1
    • 49449116792 scopus 로고    scopus 로고
    • Oxidative innate immune defenses by Nox/ Duox family NADPH oxidases
    • Rada, B., Leto, T. L. (2008) Oxidative innate immune defenses by Nox/ Duox family NADPH oxidases. Contrib. Microbiol. 15, 164-187.
    • (2008) Contrib. Microbiol. , vol.15 , pp. 164-187
    • Rada, B.1    Leto, T.L.2
  • 2
    • 0026628807 scopus 로고
    • Chronic granulomatous disease
    • Dinauer, M. C., Orkin, S. H. (1992) Chronic granulomatous disease. Annu. Rev. Med. 43, 117-124.
    • (1992) Annu. Rev. Med. , vol.43 , pp. 117-124
    • Dinauer, M.C.1    Orkin, S.H.2
  • 3
    • 47149105471 scopus 로고    scopus 로고
    • Nox enzymes in immune cells
    • Nauseef, W. M. (2008) Nox enzymes in immune cells. Semin. Immunopathol. 30, 195-208.
    • (2008) Semin. Immunopathol. , vol.30 , pp. 195-208
    • Nauseef, W.M.1
  • 4
    • 0033795342 scopus 로고    scopus 로고
    • p47(phox)-deficient NADPH oxidase defect in neutrophils of diabetic mouse strains, C57BL/6J-m db/db and db/+
    • Huang, C. K., Zhan, L., Hannigan, M. O., Ai, Y., Leto, T. L. (2000) p47(phox)-deficient NADPH oxidase defect in neutrophils of diabetic mouse strains, C57BL/6J-m db/db and db/+. J. Leukoc. Biol. 67, 210-215.
    • (2000) J. Leukoc. Biol. , vol.67 , pp. 210-215
    • Huang, C.K.1    Zhan, L.2    Hannigan, M.O.3    Ai, Y.4    Leto, T.L.5
  • 5
    • 4344591766 scopus 로고    scopus 로고
    • Enhanced autoimmunity, arthritis, and encephalomyelitis in mice with a reduced oxidative burst due to a mutation in the Ncf1 gene
    • Hultqvist, M., Olofsson, P., Holmberg, J., Bäckström, B. T., Tordsson, J., Holmdahl, R. (2004) Enhanced autoimmunity, arthritis, and encephalomyelitis in mice with a reduced oxidative burst due to a mutation in the Ncf1 gene. Proc. Natl. Acad. Sci. USA 101, 12646-12651.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12646-12651
    • Hultqvist, M.1    Olofsson, P.2    Holmberg, J.3    Bäckström, B.T.4    Tordsson, J.5    Holmdahl, R.6
  • 9
    • 0028984840 scopus 로고
    • The p47phox mouse knock-out model of chronic granulomatous disease
    • Jackson, S. H., Gallin, J. I., Holland, S. M. (1995) The p47phox mouse knock-out model of chronic granulomatous disease. J. Exp. Med. 182, 751-758.
    • (1995) J. Exp. Med. , vol.182 , pp. 751-758
    • Jackson, S.H.1    Gallin, J.I.2    Holland, S.M.3
  • 11
    • 0034658353 scopus 로고    scopus 로고
    • Superoxide prevents nitric oxide-mediated suppression of helper T lymphocytes: Decreased autoimmune encephalomyelitis in nicotinamide adenine dinucleotide phosphate oxidase knockout mice
    • Van der Veen, R. C., Dietlin, T. A., Hofman, F. M., Pen, L., Segal, B. H., Holland, S. M. (2000) Superoxide prevents nitric oxide-mediated suppression of helper T lymphocytes: decreased autoimmune encephalomyelitis in nicotinamide adenine dinucleotide phosphate oxidase knockout mice. J. Immunol. 164, 5177-5183.
    • (2000) J. Immunol. , vol.164 , pp. 5177-5183
    • Van der Veen, R.C.1    Dietlin, T.A.2    Hofman, F.M.3    Pen, L.4    Segal, B.H.5    Holland, S.M.6
  • 12
    • 0037224772 scopus 로고    scopus 로고
    • Positional identification of Ncf1 as a gene that regulates arthritis severity in rats
    • Olofsson, P., Holmberg, J., Tordsson, J., Lu, S., Akerström, B., Holmdahl, R. (2003) Positional identification of Ncf1 as a gene that regulates arthritis severity in rats. Nat. Genet. 33, 25.
    • (2003) Nat. Genet. , vol.33 , pp. 25
    • Olofsson, P.1    Holmberg, J.2    Tordsson, J.3    Lu, S.4    Akerström, B.5    Holmdahl, R.6
  • 13
    • 0030045762 scopus 로고    scopus 로고
    • Genotype-dependent variability in flow cytometric evaluation of reduced nicotinamide adenine dinucleotide phosphate oxidase function in patients with chronic granulomatous disease
    • Vowells, S. J., Fleisher, T. A., Sekhsaria, S., Alling, D. W., Maguire, T. E., Malech, H. L. (1996) Genotype-dependent variability in flow cytometric evaluation of reduced nicotinamide adenine dinucleotide phosphate oxidase function in patients with chronic granulomatous disease. J. Pediatr. 128, 104-107.
    • (1996) J. Pediatr. , vol.128 , pp. 104-107
    • Vowells, S.J.1    Fleisher, T.A.2    Sekhsaria, S.3    Alling, D.W.4    Maguire, T.E.5    Malech, H.L.6
  • 15
    • 0037089309 scopus 로고    scopus 로고
    • Creation of a genetic system for analysis of the phagocyte respiratory burst: High-level reconstitution of the NADPH oxidase in a nonhematopoietic system
    • Price, M. O., McPhail, L. C., Lambeth, J. D., Han, C. H., Knaus, U. G., Dinauer, M. C. (2002) Creation of a genetic system for analysis of the phagocyte respiratory burst: high-level reconstitution of the NADPH oxidase in a nonhematopoietic system. Blood 99, 2653-2661.
    • (2002) Blood , vol.99 , pp. 2653-2661
    • Price, M.O.1    McPhail, L.C.2    Lambeth, J.D.3    Han, C.H.4    Knaus, U.G.5    Dinauer, M.C.6
  • 16
    • 0033396672 scopus 로고    scopus 로고
    • Respiratory burst in human neutrophils
    • Dahlgren, C., Karlsson, A. (1999) Respiratory burst in human neutrophils. J. Immunol. Methods 232, 3-14.
    • (1999) J. Immunol. Methods , vol.232 , pp. 3-14
    • Dahlgren, C.1    Karlsson, A.2
  • 17
    • 0028887591 scopus 로고
    • Flow cytometric analysis of the granulocyte respiratory burst: A comparison study of fluorescent probes
    • Vowells, S. J., Sekhsaria, S., Malech, H. L., Shalit, M., Fleisher, T. A. (1995) Flow cytometric analysis of the granulocyte respiratory burst: a comparison study of fluorescent probes. J. Immunol. Methods 178, 89-97.
    • (1995) J. Immunol. Methods , vol.178 , pp. 89-97
    • Vowells, S.J.1    Sekhsaria, S.2    Malech, H.L.3    Shalit, M.4    Fleisher, T.A.5
  • 18
    • 79957475372 scopus 로고    scopus 로고
    • Positioning of a polymorphic quantitative trait nucleotide in the Ncf1 gene controlling oxidative burst response and arthritis severity in rats
    • Hultqvist, M., Sareila, O., Vilhardt, F., Norin, U., Olsson, L. M., Olofsson, P., Hellman, U., Holmdahl, R. (2011) Positioning of a polymorphic quantitative trait nucleotide in the Ncf1 gene controlling oxidative burst response and arthritis severity in rats. Antioxid. Redox Signal. 14, 2373-2383.
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 2373-2383
    • Hultqvist, M.1    Sareila, O.2    Vilhardt, F.3    Norin, U.4    Olsson, L.M.5    Olofsson, P.6    Hellman, U.7    Holmdahl, R.8
  • 19
    • 0028170628 scopus 로고
    • 156Pro¡Gln substitution in the light chain of cytochrome b558 of the human NADPH oxidase (p22-phox) leads to defective translocation of the cytosolic proteins p47-phox and p67-phox
    • Leusen, J. H., Bolscher, B. G., Hilarius, P. M., Weening, R. S., Kaulfersch, W., Seger, R. A., Roos, D., Verhoeven, A. J. (1994) 156Pro¡Gln substitution in the light chain of cytochrome b558 of the human NADPH oxidase (p22-phox) leads to defective translocation of the cytosolic proteins p47-phox and p67-phox. J. Exp. Med. 180, 2329-2334.
    • (1994) J. Exp. Med. , vol.180 , pp. 2329-2334
    • Leusen, J.H.1    Bolscher, B.G.2    Hilarius, P.M.3    Weening, R.S.4    Kaulfersch, W.5    Seger, R.A.6    Roos, D.7    Verhoeven, A.J.8
  • 20
    • 47149104660 scopus 로고    scopus 로고
    • Priming of the neutrophil NADPH oxidase activation: Role of p47phox phosphorylation and NOX2 mobilization to the plasma membrane
    • El-Benna, J., Dang, P., Gougerot-Pocidalo, M. (2008) Priming of the neutrophil NADPH oxidase activation: role of p47phox phosphorylation and NOX2 mobilization to the plasma membrane. Sem. Immunopathol. 30, 279-289.
    • (2008) Sem. Immunopathol. , vol.30 , pp. 279-289
    • El-Benna, J.1    Dang, P.2    Gougerot-Pocidalo, M.3
  • 21
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylation-induced activation of the NADPH oxidase
    • Groemping, Y., Lapouge, K., Smerdon, S. J., Rittinger, K. (2003) Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell 113, 343-355.
    • (2003) Cell , vol.113 , pp. 343-355
    • Groemping, Y.1    Lapouge, K.2    Smerdon, S.J.3    Rittinger, K.4
  • 22
    • 34548657163 scopus 로고    scopus 로고
    • Lack of reactive oxygen species breaks T cell tolerance to collagen type II and allows development of arthritis in mice
    • Hultqvist, M., Bäcklund, J., Bauer, K., Gelderman, K. A., Holmdahl, R. (2007) Lack of reactive oxygen species breaks T cell tolerance to collagen type II and allows development of arthritis in mice. J. Immunol. 179, 1431-1437.
    • (2007) J. Immunol. , vol.179 , pp. 1431-1437
    • Hultqvist, M.1    Bäcklund, J.2    Bauer, K.3    Gelderman, K.A.4    Holmdahl, R.5
  • 23
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard, K., Krause, K. H. (2007) The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 87, 245-313.
    • (2007) Physiol. Rev. , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 25
    • 0037853270 scopus 로고    scopus 로고
    • Membrane binding mechanisms of the PX domains of NADPH oxidase p40phox and p47phox
    • Stahelin, R. V., Burian, A., Bruzik, K. S., Murray, D., Cho, W. (2003) Membrane binding mechanisms of the PX domains of NADPH oxidase p40phox and p47phox. J. Biol. Chem. 278, 14469-14479.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14469-14479
    • Stahelin, R.V.1    Burian, A.2    Bruzik, K.S.3    Murray, D.4    Cho, W.5
  • 26
    • 0037446850 scopus 로고    scopus 로고
    • Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation
    • Ago, T., Kuribayashi, F., Hiroaki, H., Takeya, R., Ito, T., Kohda, D., Sumimoto, H. (2003) Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation. Proc. Natl. Acad. Sci. USA 100, 4474-4479.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4474-4479
    • Ago, T.1    Kuribayashi, F.2    Hiroaki, H.3    Takeya, R.4    Ito, T.5    Kohda, D.6    Sumimoto, H.7
  • 27
    • 0037039667 scopus 로고    scopus 로고
    • The p40phox and p47phox PX domains of NADPH oxidase target cell membranes via direct and indirect recruitment by phosphoinositides
    • Zhan, Y., Virbasius, J. V., Song, X., Pomerleau, D. P., Zhou, G. W. (2002) The p40phox and p47phox PX domains of NADPH oxidase target cell membranes via direct and indirect recruitment by phosphoinositides. J. Biol. Chem. 277, 4512-4518.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4512-4518
    • Zhan, Y.1    Virbasius, J.V.2    Song, X.3    Pomerleau, D.P.4    Zhou, G.W.5
  • 28
    • 64249137847 scopus 로고    scopus 로고
    • A region N-terminal to the tandem SH3 domain of p47phox plays a crucial role in the activation of the phagocyte NADPH oxidase
    • Taura, M., Miyano, K., Minakami, R., Kamakura, S., Takeya, R., Sumimoto, H. (2009) A region N-terminal to the tandem SH3 domain of p47phox plays a crucial role in the activation of the phagocyte NADPH oxidase. Biochem. J. 419, 329-338.
    • (2009) Biochem. J. , vol.419 , pp. 329-338
    • Taura, M.1    Miyano, K.2    Minakami, R.3    Kamakura, S.4    Takeya, R.5    Sumimoto, H.6
  • 29
    • 50149085513 scopus 로고    scopus 로고
    • Mutations in the PX-SH3A linker of p47phox decouple PI(3,4)P2 binding from NADPH oxidase activation
    • Shen, K., Sergeant, S., Hantgan, R. R., McPhail, L. C., Horita, D. A. (2008) Mutations in the PX-SH3A linker of p47phox decouple PI(3,4)P2 binding from NADPH oxidase activation. Biochemistry 47, 8855-8865.
    • (2008) Biochemistry , vol.47 , pp. 8855-8865
    • Shen, K.1    Sergeant, S.2    Hantgan, R.R.3    McPhail, L.C.4    Horita, D.A.5
  • 30
    • 0037102138 scopus 로고    scopus 로고
    • Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p
    • Kami, K., Takeya, R., Sumimoto, H., Kohda, D. (2002) Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p. EMBO J. 21, 4268-4276.
    • (2002) EMBO J. , vol.21 , pp. 4268-4276
    • Kami, K.1    Takeya, R.2    Sumimoto, H.3    Kohda, D.4
  • 31
    • 0035852956 scopus 로고    scopus 로고
    • Small angle neutron scattering and gel filtration analyses of neutrophil NADPH oxidase cytosolic factors highlight the role of the C-terminal end of p47phox in the association with p40phox
    • Grizot, S., Grandvaux, N., Fieschi, F., Faure, J., Massenet, C., Andrieu, J. P., Fuchs, A., Vignais, P. V., Timmins, P. A., Dagher, M. C., Pebay-Peyroula, E. (2001) Small angle neutron scattering and gel filtration analyses of neutrophil NADPH oxidase cytosolic factors highlight the role of the C-terminal end of p47phox in the association with p40phox. Biochemistry 40, 3127-3133.
    • (2001) Biochemistry , vol.40 , pp. 3127-3133
    • Grizot, S.1    Grandvaux, N.2    Fieschi, F.3    Faure, J.4    Massenet, C.5    Andrieu, J.P.6    Fuchs, A.7    Vignais, P.V.8    Timmins, P.A.9    Dagher, M.C.10    Pebay-Peyroula, E.11
  • 32
    • 0029835305 scopus 로고    scopus 로고
    • Interactions between cytosolic components of the NADPH oxidase: P40phox interacts with both p67phox and p47phox
    • Wientjes, F. B., Panayotou, G., Reeves, E., Segal, A. W. (1996) Interactions between cytosolic components of the NADPH oxidase: p40phox interacts with both p67phox and p47phox. Biochem. J. 317, 919-924.
    • (1996) Biochem. J. , vol.317 , pp. 919-924
    • Wientjes, F.B.1    Panayotou, G.2    Reeves, E.3    Segal, A.W.4
  • 33
    • 0034486070 scopus 로고    scopus 로고
    • The identification of conserved interactions within the SH3 domain by alignment of sequences and structures
    • Larson, S. M., Davidson, A. R. (2000) The identification of conserved interactions within the SH3 domain by alignment of sequences and structures. Protein Sci. 9, 2170-2180.
    • (2000) Protein Sci. , vol.9 , pp. 2170-2180
    • Larson, S.M.1    Davidson, A.R.2
  • 34
    • 33646784346 scopus 로고    scopus 로고
    • Activation of the superoxide-producing phagocyte NADPH oxidase requires co-operation between the tandem SH3 domains of p47phox in recognition of a polyproline type II helix and an adjacent α-helix of p22phox
    • Nobuhisa, I., Takeya, R., Ogura, K., Ueno, N., Kohda, D., Inagaki, F., Sumimoto, H. (2006) Activation of the superoxide-producing phagocyte NADPH oxidase requires co-operation between the tandem SH3 domains of p47phox in recognition of a polyproline type II helix and an adjacent α-helix of p22phox. Biochem. J. 396, 183-192.
    • (2006) Biochem. J. , vol.396 , pp. 183-192
    • Nobuhisa, I.1    Takeya, R.2    Ogura, K.3    Ueno, N.4    Kohda, D.5    Inagaki, F.6    Sumimoto, H.7
  • 35
    • 33645641343 scopus 로고    scopus 로고
    • NMR solution structure of the tandem Src homology 3 domains of p47phox complexed with a p22phox-derived proline-rich peptide
    • Ogura, K., Nobuhisa, I., Yuzawa, S., Takeya, R., Torikai, S., Saikawa, K., Sumimoto, H., Inagaki, F. (2006) NMR solution structure of the tandem Src homology 3 domains of p47phox complexed with a p22phox-derived proline-rich peptide. J. Biol. Chem. 281, 3660-3668.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3660-3668
    • Ogura, K.1    Nobuhisa, I.2    Yuzawa, S.3    Takeya, R.4    Torikai, S.5    Saikawa, K.6    Sumimoto, H.7    Inagaki, F.8
  • 36
    • 33745027665 scopus 로고    scopus 로고
    • Small-angle X-ray scattering reveals an extended organization for the autoinhibitory resting state of the p47(phox) modular protein
    • Durand, D., Cannella, D., Dubosclard, V., Pebay-Peyroula, E., Vachette, P., Fieschi, F. (2006) Small-angle X-ray scattering reveals an extended organization for the autoinhibitory resting state of the p47(phox) modular protein. Biochemistry 45, 7185-7193.
    • (2006) Biochemistry , vol.45 , pp. 7185-7193
    • Durand, D.1    Cannella, D.2    Dubosclard, V.3    Pebay-Peyroula, E.4    Vachette, P.5    Fieschi, F.6
  • 37
    • 2942672401 scopus 로고    scopus 로고
    • A molecular mechanism for autoinhibition of the tandem SH3 domains of p47phox, the regulatory subunit of the phagocyte NADPH oxidase
    • Yuzawa, S., Suzuki, N. N., Fujioka, Y., Ogura, K., Sumimoto, H., Inagaki, F. (2004) A molecular mechanism for autoinhibition of the tandem SH3 domains of p47phox, the regulatory subunit of the phagocyte NADPH oxidase. Genes Cells 9, 443-456.
    • (2004) Genes Cells , vol.9 , pp. 443-456
    • Yuzawa, S.1    Suzuki, N.N.2    Fujioka, Y.3    Ogura, K.4    Sumimoto, H.5    Inagaki, F.6
  • 39
    • 0036791737 scopus 로고    scopus 로고
    • Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction
    • Karathanassis, D., Stahelin, R. V., Bravo, J., Perisic, O., Pacold, C. M., Cho, W., Williams, R. L. (2002) Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction. EMBO J. 21, 5057-5068.
    • (2002) EMBO J. , vol.21 , pp. 5057-5068
    • Karathanassis, D.1    Stahelin, R.V.2    Bravo, J.3    Perisic, O.4    Pacold, C.M.5    Cho, W.6    Williams, R.L.7
  • 40
    • 0034995037 scopus 로고    scopus 로고
    • Solution structure of the PX domain, a target of the SH3 domain
    • Hiroaki, H., Ago, T., Ito, T., Sumimoto, H., Kohda, D. (2001) Solution structure of the PX domain, a target of the SH3 domain. Nat. Struct. Biol. 8, 526-530.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 526-530
    • Hiroaki, H.1    Ago, T.2    Ito, T.3    Sumimoto, H.4    Kohda, D.5


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