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Volumn 1, Issue 6, 2009, Pages 543-555

The domain organization of p67, a protein required for activation of the superoxide-producing NADPH oxidase in phagocytes

Author keywords

Domain organization; Innate immunity; NADPH oxidase; P67phox; Phagocyte; Small angle X ray scattering

Indexed keywords

MONOMER; PROTEIN P40; PROTEIN P47; PROTEIN P67; PROTEIN SH3; RAC PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; SUPEROXIDE;

EID: 70350337947     PISSN: 1662811X     EISSN: 16628128     Source Type: Journal    
DOI: 10.1159/000235656     Document Type: Article
Times cited : (20)

References (45)
  • 1
    • 33344468233 scopus 로고    scopus 로고
    • Neutrophils and immunity: Challenges and opportunities
    • Nathan C: Neutrophils and immunity: challenges and opportunities. Nat Rev Immunol 2006; 6: 173-182.
    • (2006) Nat Rev Immunol , vol.6 , pp. 173-182
    • Nathan, C.1
  • 2
    • 34548588559 scopus 로고    scopus 로고
    • How human neutrophils kill and degrade microbes: An integrated view
    • Nauseef WM: How human neutrophils kill and degrade microbes: An integrated view. Immunol Rev 2007; 219: 88-102.
    • (2007) Immunol Rev , vol.219 , pp. 88-102
    • Nauseef, W.M.1
  • 3
    • 0347711117 scopus 로고    scopus 로고
    • NADPH oxidases: Not just for leukocytes anymore!
    • Bokoch GM, Knaus UG: NADPH oxidases: not just for leukocytes anymore! Trends Biochem Sci 2003; 28: 502-508.
    • (2003) Trends Biochem Sci , vol.28 , pp. 502-508
    • Bokoch, G.M.1    Knaus, U.G.2
  • 4
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth JD: NOX enzymes and the biology of reactive oxygen. Nat Rev Immunol 2004; 4: 181-189.
    • (2004) Nat Rev Immunol , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 5
    • 10644262971 scopus 로고    scopus 로고
    • The Nox family of NAD(P)H oxidases: Host defense and beyond
    • Geiszt M, Leto TL: The Nox family of NAD(P)H oxidases: host defense and beyond. J Biol Chem 2004; 279: 51715-51718.
    • (2004) J Biol Chem , vol.279 , pp. 51715-51718
    • Geiszt, M.1    Leto, T.L.2
  • 6
    • 15944372262 scopus 로고    scopus 로고
    • Activation and assembly of the NADPH oxidase: A structural perspective
    • Groemping Y, Rittinger K: Activation and assembly of the NADPH oxidase: A structural perspective. Biochem J 2005; 386: 401-416.
    • (2005) Biochem J , vol.386 , pp. 401-416
    • Groemping, Y.1    Rittinger, K.2
  • 7
    • 34547906543 scopus 로고    scopus 로고
    • Opening the black box: Lessons from cell-free systems on the phagocyte NADPH-oxidase
    • Dagher MC, Pick E: Opening the black box: lessons from cell-free systems on the phagocyte NADPH-oxidase. Biochimie 2007; 89: 1123-1132.
    • (2007) Biochimie , vol.89 , pp. 1123-1132
    • Dagher, M.C.1    Pick, E.2
  • 8
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard K, Krause K-H: The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev 2007; 87: 245-313.
    • (2007) Physiol Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.-H.2
  • 9
    • 44949106317 scopus 로고    scopus 로고
    • Structure, regulation and evolution of Nox-family NADPH oxidases that produce reactive oxygen species
    • Sumimoto H: Structure, regulation and evolution of Nox-family NADPH oxidases that produce reactive oxygen species. FEBS J 2008; 275: 3249-3277.
    • (2008) FEBS J , vol.275 , pp. 3249-3277
    • Sumimoto, H.1
  • 10
    • 0029812877 scopus 로고    scopus 로고
    • NADPH oxidase activity is independent of p47 phox in vitro
    • Freeman JL, Lambeth JD: NADPH oxidase activity is independent of p47 phox in vitro. J Biol Chem 1996; 271: 22578-22582.
    • (1996) J Biol Chem , vol.271 , pp. 22578-22582
    • Freeman, J.L.1    Lambeth, J.D.2
  • 11
    • 0029828538 scopus 로고    scopus 로고
    • The cytosolic component p47 phox is not a sine qua non participant in the activation of NADPH oxidase but is required for optimal superoxide production
    • Koshkin V, Lotan O, Pick E: The cytosolic component p47 phox is not a sine qua non participant in the activation of NADPH oxidase but is required for optimal superoxide production. J Biol Chem 1996; 271: 30326-30329.
    • (1996) J Biol Chem , vol.271 , pp. 30326-30329
    • Koshkin, V.1    Lotan, O.2    Pick, E.3
  • 12
    • 18744403007 scopus 로고    scopus 로고
    • The adaptor protein p40 phox as a positive regulator of the superoxide-producing phagocyte oxidase
    • Kuribayashi F, Nunoi H, Wakamatsu K, Tsunawaki S, Sato K, Ito T, Sumimoto H: The adaptor protein p40 phox as a positive regulator of the superoxide-producing phagocyte oxidase. EMBO J 2002; 21: 6312-6320.
    • (2002) EMBO J , vol.21 , pp. 6312-6320
    • Kuribayashi, F.1    Nunoi, H.2    Wakamatsu, K.3    Tsunawaki, S.4    Sato, K.5    Ito, T.6    Sumimoto, H.7
  • 13
  • 14
    • 33749317192 scopus 로고    scopus 로고
    • PtdIns3P binding to the PX domain of p40 phox is a physiological signal in NADPH oxidase activation
    • Ellson C, Davidson K, Anderson K, Stephens LR, Hawkins PT: PtdIns3P binding to the PX domain of p40 phox is a physiological signal in NADPH oxidase activation. EMBO J 2006; 25: 4468-4478.
    • (2006) EMBO J , vol.25 , pp. 4468-4478
    • Ellson, C.1    Davidson, K.2    Anderson, K.3    Stephens, L.R.4    Hawkins, P.T.5
  • 15
    • 0041625934 scopus 로고    scopus 로고
    • PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62
    • Wilson MI, Gill DJ, Perisic O, Quinn MT, Williams RL: PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62. Mol Cell 2003; 12: 39-50.
    • (2003) Mol Cell , vol.12 , pp. 39-50
    • Wilson, M.I.1    Gill, D.J.2    Perisic, O.3    Quinn, M.T.4    Williams, R.L.5
  • 16
    • 36749060688 scopus 로고    scopus 로고
    • Structure and function of the PB1 domain, a protein interaction module conserved in animals, fungi, amoebas, and plants
    • Sumimoto H, Kamakura S, Ito T: Structure and function of the PB1 domain, a protein interaction module conserved in animals, fungi, amoebas, and plants. Sci STKE 2007; 2007:re6.
    • (2007) Sci STKE , vol.2007
    • Sumimoto, H.1    Kamakura, S.2    Ito, T.3
  • 17
    • 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: Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67 phox , Grb2 and Pex13p. EMBO J 2002; 21: 4268-4276.
    • (2002) EMBO J , vol.21 , pp. 4268-4276
    • Kami, K.1    Takeya, R.2    Sumimoto, H.3    Kohda, D.4
  • 18
    • 17144412976 scopus 로고    scopus 로고
    • Effects of p47 phox C terminus phosphorylations on binding interactions with p40 phox and p67 phox : SSStructural and functional comparison of p40 phox and p67 phox SH3 domains
    • Massenet C, Chenavas S, Cohen-Addad C, Dagher MC, Brandolin G, Pebay-Peyroula E, Fieschi F: Effects of p47 phox C terminus phosphorylations on binding interactions with p40 phox and p67 phox : structural and functional comparison of p40 phox and p67 phox SH3 domains. J Biol Chem 2005; 280: 13752-13761.
    • (2005) J Biol Chem , vol.280 , pp. 13752-13761
    • Massenet, C.1    Chenavas, S.2    Cohen-Addad, C.3    Dagher, M.C.4    Brandolin, G.5    Pebay-Peyroula, E.6    Fieschi, F.7
  • 19
    • 28444437723 scopus 로고    scopus 로고
    • A region C-terminal to the prolinerich core of p47 phox regulates activation of the phagocyte NADPH oxidase by interacting with the C-terminal SH3 domain of p67 phox
    • Mizuki K, Takeya R, Kuribayashi F, Nobuhisa I, Kohda D, Nunoi H, Takeshige K, Sumimoto H: A region C-terminal to the prolinerich core of p47 phox regulates activation of the phagocyte NADPH oxidase by interacting with the C-terminal SH3 domain of p67 phox . Arch Biochem Biophys 2005; 444: 185-194.
    • (2005) Arch Biochem Biophys , vol.444 , pp. 185-194
    • Mizuki, K.1    Takeya, R.2    Kuribayashi, F.3    Nobuhisa, I.4    Kohda, D.5    Nunoi, H.6    Takeshige, K.7    Sumimoto, H.8
  • 20
    • 0037155889 scopus 로고    scopus 로고
    • Architecture of the p40-p47-p67 phox complex in the resting state of the NADPH oxidase: A central role for p67 phox
    • Lapouge K, Smith SJ, Groemping Y, Rittinger K: Architecture of the p40-p47-p67 phox complex in the resting state of the NADPH oxidase: A central role for p67 phox . J Biol Chem 2002; 277: 10121-10128.
    • (2002) J Biol Chem , vol.277 , pp. 10121-10128
    • Lapouge, K.1    Smith, S.J.2    Groemping, Y.3    Rittinger, K.4
  • 21
    • 0033609785 scopus 로고    scopus 로고
    • Tetratricopeptide repeat (TPR) motifs of p67 phox participate in interaction with the small GTPase Rac and activation of the phagocyte NADPH oxidase
    • Koga H, Terasawa H, Nunoi H, Takeshige K, Inagaki F, Sumimoto H: Tetratricopeptide repeat (TPR) motifs of p67 phox participate in interaction with the small GTPase Rac and activation of the phagocyte NADPH oxidase. J Biol Chem 1999; 274: 25051-25060.
    • (1999) J Biol Chem , vol.274 , pp. 25051-25060
    • Koga, H.1    Terasawa, H.2    Nunoi, H.3    Takeshige, K.4    Inagaki, F.5    Sumimoto, H.6
  • 23
    • 58149479248 scopus 로고    scopus 로고
    • Role for the first SH3 domain of p67 phox in activation of superoxide-producing NADPH oxidases
    • Maehara Y, Miyano K, Sumimoto H: Role for the first SH3 domain of p67 phox in activation of superoxide-producing NADPH oxidases. Biochem Biophys Res Commun 2009; 379: 589-593.
    • (2009) Biochem Biophys Res Commun , vol.379 , pp. 589-593
    • Maehara, Y.1    Miyano, K.2    Sumimoto, H.3
  • 24
    • 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 p47 phox in the association with p40 phox
    • Grizot S, Grandvaux N, Fieschi F, Fraué J, Massenet C, Andrieu JP, Fuchs A, Vignais PV, Timmins PA, Dagher MC, Pebay-Peyroula E: Small angle neutron scattering and gel filtration analyses of neutrophil NADPH oxidase cytosolic factors highlight the role of the C-terminal end of p47 phox in the association with p40 phox . Biochemistry 2001; 40: 3127-3133.
    • (2001) Biochemistry , vol.40 , pp. 3127-3133
    • Grizot, S.1    Grandvaux, N.2    Fieschi, F.3    Fraué, 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
  • 25
    • 33745027665 scopus 로고    scopus 로고
    • Smallangle 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: Smallangle X-ray scattering reveals an extended organization for the autoinhibitory resting state of the p47 phox modular protein. Biochemistry 2006; 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
  • 27
    • 2942746422 scopus 로고    scopus 로고
    • Binding of FAD to cytochrome b 558 is facilitated during activation of the phagocyte NADPH oxidase, leading to superoxide production
    • Hashida S, Yuzawa S, Suzuki NN, Fujioka Y, Takikawa T, Sumimoto H, Inagaki F, Fujii H: Binding of FAD to cytochrome b 558 is facilitated during activation of the phagocyte NADPH oxidase, leading to superoxide production. J Biol Chem 2004; 279: 26378-26386.
    • (2004) J Biol Chem , vol.279 , pp. 26378-26386
    • Hashida, S.1    Yuzawa, S.2    Suzuki, N.N.3    Fujioka, Y.4    Takikawa, T.5    Sumimoto, H.6    Inagaki, F.7    Fujii, H.8
  • 28
    • 0034009520 scopus 로고    scopus 로고
    • Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck P: Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys J 2000; 78: 1606-1619.
    • (2000) Biophys J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 29
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins; In Harding SE, Rowe AJ, Horton JC (eds): Analytical Ultracentrifugation in Biochemistry and Polymer Science
    • Laue TM, Shah BD, Ridgeway TM, Pelletier SL: Computer-aided interpretation of analytical sedimentation data for proteins; in Harding SE, Rowe AJ, Horton JC (eds): Analytical Ultracentrifugation in Biochemistry and Polymer Science. Cambridge, Royal Society of Chemistry, 1992, pp 90-125.
    • (1992) Cambridge, Royal Society of Chemistry , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 31
    • 0022160183 scopus 로고
    • Aggregation of bovine serum albumin upon cleavage of its disulfide bonds, studied by the time-resolved small-angle X-ray scattering technique with synchrotron radiation
    • Ueki T, Hiragi Y, Kataoka M, Inoko Y, Amemiya Y, Izumi Y, Tagawa H, Muroga Y: Aggregation of bovine serum albumin upon cleavage of its disulfide bonds, studied by the time-resolved small-angle X-ray scattering technique with synchrotron radiation. Biophys Chem 1985; 23: 115-124.
    • (1985) Biophys Chem , vol.23 , pp. 115-124
    • Ueki, T.1    Hiragi, Y.2    Kataoka, M.3    Inoko, Y.4    Amemiya, Y.5    Izumi, Y.6    Tagawa, H.7    Muroga, Y.8
  • 32
    • 0000739195 scopus 로고
    • Melittin binding causes a large calcium- dependent conformational change in calmodulin
    • Kataoka M, Head JF, Seaton BA, Engelman DM: Melittin binding causes a large calcium- dependent conformational change in calmodulin. Proc Natl Acad Sci USA 1989; 86: 6944-6948.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6944-6948
    • Kataoka, M.1    Head, J.F.2    Seaton, B.A.3    Engelman, D.M.4
  • 35
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun DI: Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Cryst 1992; 25: 495-503.
    • (1992) J Appl Cryst , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 36
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun DI: Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 1999; 76: 2879-2886.
    • (1999) Biophys J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 37
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun DI, Petoukhov MV, Koch MHJ: Determination of domain structure of proteins from X-ray solution scattering. Biophys J 2001; 80: 2946-2953.
    • (2001) Biophys J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 38
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high-and low-resolution structural models
    • Kozin MB, Svergun DI: Automated matching of high-and low-resolution structural models: J Appl Cryst 2002; 34: 33-41.
    • (2002) J Appl Cryst , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 39
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, Svergun DI: Uniqueness of ab initio shape determination in small-angle scattering. J Appl Cryst 2003; 36: 860-864.
    • (2003) J Appl Cryst , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 40
    • 32144436424 scopus 로고    scopus 로고
    • Regulation of superoxide-producing NADPH oxidases in nonphagocytic cells
    • DOI 10.1016/S0076-6879(06)06034-4, PII S0076687906060344, 34, Regulators and Effectors of Small GTPases: Rho Family
    • Takeya R, Ueno N, Sumimoto H: Regulation of superoxide-producing NADPH oxidases in nonphagocytic cells. Methods Enzymol 2006; 406: 456-468. (Pubitemid 43207459)
    • (2006) Methods in Enzymology , vol.406 , pp. 456-468
    • Takeya, R.1    Ueno, N.2    Sumimoto, H.3
  • 41
    • 34547852395 scopus 로고    scopus 로고
    • Role of the small GTPase Rac in p22 phox -dependent NADPH oxidases
    • Miyano K, Sumimoto H: Role of the small GTPase Rac in p22 phox -dependent NADPH oxidases. Biochimie 2007; 89: 1133-1144.
    • (2007) Biochimie , vol.89 , pp. 1133-1144
    • Miyano, K.1    Sumimoto, H.2
  • 42
    • 0032479170 scopus 로고    scopus 로고
    • Regulation of the neutrophil respiratory burst oxidase: Ientification of an activation domain in p67 phox
    • Han C-H, Freeman JL, Lee T, Motalebi SA, Lambeth JD: Regulation of the neutrophil respiratory burst oxidase: Identification of an activation domain in p67 phox . J Biol Chem 1998; 273: 16663-16668.
    • (1998) J Biol Chem , vol.273 , pp. 16663-16668
    • Han, C.-H.1    Freeman, J.L.2    Lee, T.3    Motalebi, S.A.4    Lambeth, J.D.5
  • 43
    • 0035421216 scopus 로고    scopus 로고
    • Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions
    • Ito T, Matsui Y, Ago T, Ota K, Sumimoto H: Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions. EMBO J 2001; 20: 3938-3946.
    • (2001) EMBO J , vol.20 , pp. 3938-3946
    • Ito, T.1    Matsui, Y.2    Ago, T.3    Ota, K.4    Sumimoto, H.5
  • 45
    • 7944223078 scopus 로고    scopus 로고
    • Structure and regulation of Src family kinases
    • Boggon TJ, Eck MJ: Structure and regulation of Src family kinases. Oncogene 2004; 23: 7918-7927.
    • (2004) Oncogene , vol.23 , pp. 7918-7927
    • Boggon, T.J.1    Eck, M.J.2


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