메뉴 건너뛰기




Volumn 89, Issue 9, 2007, Pages 1133-1144

Role of the small GTPase Rac in p22phox-dependent NADPH oxidases

Author keywords

gp91phox; Nox1; Nox3; p67phox; Rac

Indexed keywords

GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PROTEIN NOXA; PROTEIN P22; PROTEIN P47; PROTEIN P67; RAC PROTEIN; RAC1 PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

EID: 34547852395     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2007.05.003     Document Type: Article
Times cited : (80)

References (56)
  • 1
    • 0036710445 scopus 로고    scopus 로고
    • The superoxide-generating NADPH oxidase: structural aspects and activation mechanism
    • Vignais P.V. The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell. Mol. Life Sci. 59 (2002) 1428-1459
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1428-1459
    • Vignais, P.V.1
  • 2
    • 0347711117 scopus 로고    scopus 로고
    • NADPH oxidases: not just for leukocytes anymore!
    • Bokoch G.M., and Knaus U.G. NADPH oxidases: not just for leukocytes anymore!. Trends Biochem. Sci. 28 (2003) 502-508
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 502-508
    • Bokoch, G.M.1    Knaus, U.G.2
  • 3
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth J.D. NOX enzymes and the biology of reactive oxygen. Nat. Rev. Immunol. 4 (2004) 181-189
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 4
    • 10644262971 scopus 로고    scopus 로고
    • The Nox family of NAD(P)H oxidases: host defense and beyond
    • Geiszt M., and Leto T.L. The Nox family of NAD(P)H oxidases: host defense and beyond. J. Biol. Chem. 279 (2004) 51715-51718
    • (2004) J. Biol. Chem. , vol.279 , pp. 51715-51718
    • Geiszt, M.1    Leto, T.L.2
  • 5
    • 27544443327 scopus 로고    scopus 로고
    • Molecular composition and regulation of the Nox family NAD(P)H oxidases
    • Sumimoto H., Miyano K., and Takeya R. Molecular composition and regulation of the Nox family NAD(P)H oxidases. Biochem. Biophys. Res. Commun. 338 (2005) 677-686
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 677-686
    • Sumimoto, H.1    Miyano, K.2    Takeya, R.3
  • 6
    • 8644255770 scopus 로고    scopus 로고
    • Assembly of the phagocyte NADPH oxidase
    • Nauseef W.M. Assembly of the phagocyte NADPH oxidase. Histochem. Cell Biol. 122 (2004) 277-291
    • (2004) Histochem. Cell Biol. , vol.122 , pp. 277-291
    • Nauseef, W.M.1
  • 7
    • 4744349398 scopus 로고    scopus 로고
    • Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases
    • Quinn M.T., and Gauss K.A. Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases. J. Leukoc. Biol. 76 (2004) 760-781
    • (2004) J. Leukoc. Biol. , vol.76 , pp. 760-781
    • Quinn, M.T.1    Gauss, K.A.2
  • 18
    • 0027973549 scopus 로고
    • I. de Mendez, Assembly of the phagocyte NADPH oxidase: binding of Src homology 3 domains to proline-rich targets
    • Leto T.L., and Adams A.G. I. de Mendez, Assembly of the phagocyte NADPH oxidase: binding of Src homology 3 domains to proline-rich targets. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 10650-10654
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 10650-10654
    • Leto, T.L.1    Adams, A.G.2
  • 19
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylation-induced activation of the NADPH oxidase
    • Groemping Y., Lapouge K., Smerdon S.J., and Rittinger K. Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell 113 (2003) 343-355
    • (2003) Cell , vol.113 , pp. 343-355
    • Groemping, Y.1    Lapouge, K.2    Smerdon, S.J.3    Rittinger, K.4
  • 24
    • 0035877848 scopus 로고    scopus 로고
    • phox: structure at 1.8 Å resolution and biochemical characterizations of the A128V mutant implicated in chronic granulomatous disease
    • phox: structure at 1.8 Å resolution and biochemical characterizations of the A128V mutant implicated in chronic granulomatous disease. J. Biol. Chem. 276 (2001) 21627-21631
    • (2001) J. Biol. Chem. , vol.276 , pp. 21627-21631
    • Grizot, S.1    Fieschi, F.2    Dagher, M.C.3    Pebay-Peyroula, E.4
  • 25
    • 8544270180 scopus 로고    scopus 로고
    • Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase
    • Ambasta R.K., Kumar P., Griendling K.K., Schmidt H.H., Busse R., and Brandes R.P. Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase. J. Biol. Chem. 279 (2004) 45935-45941
    • (2004) J. Biol. Chem. , vol.279 , pp. 45935-45941
    • Ambasta, R.K.1    Kumar, P.2    Griendling, K.K.3    Schmidt, H.H.4    Busse, R.5    Brandes, R.P.6
  • 27
    • 0038789165 scopus 로고    scopus 로고
    • Two novel proteins activate superoxide generation by the NADPH oxidase NOX1
    • Bánfi B., Clark R.A., Steger K., and Krause K.-H. Two novel proteins activate superoxide generation by the NADPH oxidase NOX1. J. Biol. Chem. 278 (2003) 3510-3513
    • (2003) J. Biol. Chem. , vol.278 , pp. 3510-3513
    • Bánfi, B.1    Clark, R.A.2    Steger, K.3    Krause, K.-H.4
  • 28
    • 0038036799 scopus 로고    scopus 로고
    • phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells
    • phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells. J. Biol. Chem. 278 (2003) 20006-20012
    • (2003) J. Biol. Chem. , vol.278 , pp. 20006-20012
    • Geiszt, M.1    Lekstrom, K.2    Witta, J.3    Leto, T.L.4
  • 29
    • 1042289744 scopus 로고    scopus 로고
    • NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain
    • Cheng G., and Lambeth J.D. NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain. J. Biol. Chem. 279 (2004) 4737-4742
    • (2004) J. Biol. Chem. , vol.279 , pp. 4737-4742
    • Cheng, G.1    Lambeth, J.D.2
  • 30
    • 33746848094 scopus 로고    scopus 로고
    • Direct involvement of the small GTPase Rac in activation of the superoxide-producing NADPH oxidase Nox1
    • Miyano K., Ueno N., Takeya R., and Sumimoto H. Direct involvement of the small GTPase Rac in activation of the superoxide-producing NADPH oxidase Nox1. J. Biol. Chem. 281 (2006) 21857-21868
    • (2006) J. Biol. Chem. , vol.281 , pp. 21857-21868
    • Miyano, K.1    Ueno, N.2    Takeya, R.3    Sumimoto, H.4
  • 31
    • 33644750712 scopus 로고    scopus 로고
    • Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-based NADPH oxidases
    • Ueyama T., Geiszt M., and Leto T.L. Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-based NADPH oxidases. Mol. Cell. Biol. 26 (2006) 2160-2174
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2160-2174
    • Ueyama, T.1    Geiszt, M.2    Leto, T.L.3
  • 32
    • 33745815084 scopus 로고    scopus 로고
    • Nox1-dependent reactive oxygen generation is regulated by Rac1
    • Cheng G., Diebold B.A., Hughes Y., and Lambeth J.D. Nox1-dependent reactive oxygen generation is regulated by Rac1. J. Biol. Chem. 281 (2006) 17718-17726
    • (2006) J. Biol. Chem. , vol.281 , pp. 17718-17726
    • Cheng, G.1    Diebold, B.A.2    Hughes, Y.3    Lambeth, J.D.4
  • 36
    • 26244444476 scopus 로고    scopus 로고
    • Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases
    • Martyn K.D., Frederick L.M., von Loehneysen K., Dinauer M.C., and Knaus U.G. Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases. Cell. Signal 18 (2006) 69-82
    • (2006) Cell. Signal , vol.18 , pp. 69-82
    • Martyn, K.D.1    Frederick, L.M.2    von Loehneysen, K.3    Dinauer, M.C.4    Knaus, U.G.5
  • 37
    • 24744468043 scopus 로고    scopus 로고
    • phox are dominant inhibitors of Nox1- and Nox2-dependent reactive oxygen generation
    • phox are dominant inhibitors of Nox1- and Nox2-dependent reactive oxygen generation. J. Biol. Chem. 280 (2005) 31859-31869
    • (2005) J. Biol. Chem. , vol.280 , pp. 31859-31869
    • Kawahara, T.1    Ritsick, D.2    Cheng, G.3    Lambeth, J.D.4
  • 42
    • 32144436424 scopus 로고    scopus 로고
    • Regulation of superoxide-producing NADPH oxidases in nonphagocytic cells
    • Takeya R., Ueno N., and Sumimoto H. Regulation of superoxide-producing NADPH oxidases in nonphagocytic cells. Methods Enzymol. 406 (2006) 456-468
    • (2006) Methods Enzymol. , vol.406 , pp. 456-468
    • Takeya, R.1    Ueno, N.2    Sumimoto, H.3
  • 43
    • 0020642791 scopus 로고
    • 2 production by macrophages and neutrophils with homovanillic acid and horse-radish peroxidase
    • 2 production by macrophages and neutrophils with homovanillic acid and horse-radish peroxidase. J. Immunol. Methods 63 (1983) 347-357
    • (1983) J. Immunol. Methods , vol.63 , pp. 347-357
    • Ruch, W.1    Cooper, P.H.2    Baggiolini, M.3
  • 44
    • 0033580822 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase-dependent and -independent activation of the small GTPase Rac2 in human neutrophils
    • Akasaki T., Koga H., and Sumimoto H. Phosphoinositide 3-kinase-dependent and -independent activation of the small GTPase Rac2 in human neutrophils. J. Biol. Chem. 274 (1999) 18055-18059
    • (1999) J. Biol. Chem. , vol.274 , pp. 18055-18059
    • Akasaki, T.1    Koga, H.2    Sumimoto, H.3
  • 45
    • 0024425981 scopus 로고
    • a novel ras-related family of proteins that are botulinum toxin substrates
    • Didsbury J., Weber R.F., Bokoch G.M., Evans T., and Snydermanrac R. a novel ras-related family of proteins that are botulinum toxin substrates. J. Biol. Chem. 264 (1989) 16378-16382
    • (1989) J. Biol. Chem. , vol.264 , pp. 16378-16382
    • Didsbury, J.1    Weber, R.F.2    Bokoch, G.M.3    Evans, T.4    Snydermanrac, R.5
  • 46
    • 12544259676 scopus 로고    scopus 로고
    • Rac GTPase isoform-specific regulation of NADPH oxidase and chemotaxis in murine neutrophils in vivo. Role of the C-terminal polybasic domain
    • Yamauchi A., Marchal C.C., Molitoris J., Pech N., Knaus U., Towe J., Atkinson S.J., and Dinauer M.C. Rac GTPase isoform-specific regulation of NADPH oxidase and chemotaxis in murine neutrophils in vivo. Role of the C-terminal polybasic domain. J. Biol. Chem. 280 (2005) 953-964
    • (2005) J. Biol. Chem. , vol.280 , pp. 953-964
    • Yamauchi, A.1    Marchal, C.C.2    Molitoris, J.3    Pech, N.4    Knaus, U.5    Towe, J.6    Atkinson, S.J.7    Dinauer, M.C.8
  • 49
    • 0029864685 scopus 로고    scopus 로고
    • Mechanisms of NADPH oxidase activation: translocation of p40phox, Rac1 and Rac2 from the cytosol to the membranes in human neutrophils lacking p47phox or p67phox
    • Dusi S., Donini M., and Rossi F. Mechanisms of NADPH oxidase activation: translocation of p40phox, Rac1 and Rac2 from the cytosol to the membranes in human neutrophils lacking p47phox or p67phox. Biochem. J. 314 (1996) 409-412
    • (1996) Biochem. J. , vol.314 , pp. 409-412
    • Dusi, S.1    Donini, M.2    Rossi, F.3
  • 54
    • 33750897683 scopus 로고    scopus 로고
    • Regulation of novel superoxide-producing NAD(P)H oxidases
    • Takeya R., and Sumimoto H. Regulation of novel superoxide-producing NAD(P)H oxidases. Antioxid. Redox Signal 8 (2006) 1523-1532
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 1523-1532
    • Takeya, R.1    Sumimoto, H.2
  • 55
    • 33748622822 scopus 로고    scopus 로고
    • Insulin-induced vascular endothelial growth factor expression is mediated by the NADPH oxidase NOX3
    • Carnesecchi S., Carpentier J.L., Foti M., and Szanto I. Insulin-induced vascular endothelial growth factor expression is mediated by the NADPH oxidase NOX3. Exp. Cell Res. 312 (2006) 3413-3424
    • (2006) Exp. Cell Res. , vol.312 , pp. 3413-3424
    • Carnesecchi, S.1    Carpentier, J.L.2    Foti, M.3    Szanto, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.