메뉴 건너뛰기




Volumn 5, Issue 5, 2010, Pages

Regulation of NOXO1 activity through reversible interactions with p22phox and NOXA1

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN NOXA1; PROTEIN NOXO1; PROTEIN P22; PROTEIN SH3; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE ACTIVATING PROTEIN 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE ORGANIZING PROTEIN 1; REGULATOR PROTEIN; SUPEROXIDE; UNCLASSIFIED DRUG;

EID: 77956297094     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0010478     Document Type: Article
Times cited : (59)

References (44)
  • 2
    • 10644262971 scopus 로고    scopus 로고
    • The Nox family of NAD(P)H oxidases: Host defense and beyond
    • Geiszt M, Leto TL (2004) The Nox family of NAD(P)H oxidases: host defense and beyond. J Biol Chem 279: 51715-51718.
    • (2004) J Biol Chem , vol.279 , pp. 51715-51718
    • Geiszt, M.1    Leto, T.L.2
  • 3
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth JD (2004) NOX enzymes and the biology of reactive oxygen. Nat Rev Immunol 4: 181-189.
    • (2004) Nat Rev Immunol , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 4
    • 9144257277 scopus 로고    scopus 로고
    • Tissue distribution and putative physiological function of NOX family NADPH oxidases
    • Krause KH (2004) Tissue distribution and putative physiological function of NOX family NADPH oxidases. Jpn J Infect Dis 57: S28-29.
    • (2004) Jpn J Infect Dis , vol.57
    • Krause, K.H.1
  • 5
    • 27544443327 scopus 로고    scopus 로고
    • Molecular composition and regulation of the Nox family NAD(P)H oxidases
    • Sumimoto H, Miyano K, Takeya R (2005) Molecular composition and regulation of the Nox family NAD(P)H oxidases. Biochem Biophys Res Commun 338: 677-686.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 677-686
    • Sumimoto, H.1    Miyano, K.2    Takeya, R.3
  • 6
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard K, Krause KH (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
  • 8
    • 0036710445 scopus 로고    scopus 로고
    • The superoxide-generating NADPH oxidase: Structural aspects and activation mechanism
    • Vignais PV (2002) The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell Mol Life Sci 59: 1428-1459.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1428-1459
    • Vignais, P.V.1
  • 9
    • 3042527868 scopus 로고    scopus 로고
    • The NADPH oxidase of professional phagocytes- prototype of the NOX electron transport chain systems
    • Cross AR, Segal AW (2004) The NADPH oxidase of professional phagocytes- prototype of the NOX electron transport chain systems. Biochim Biophys Acta 1657: 1-22.
    • (2004) Biochim Biophys Acta , vol.1657 , pp. 1-22
    • Cross, A.R.1    Segal, A.W.2
  • 10
    • 8644255770 scopus 로고    scopus 로고
    • Assembly of the phagocyte NADPH oxidase
    • Nauseef WM (2004) Assembly of the phagocyte NADPH oxidase. Histochem Cell Biol 122: 277-291.
    • (2004) Histochem Cell Biol , vol.122 , pp. 277-291
    • Nauseef, W.M.1
  • 11
    • 0033517275 scopus 로고    scopus 로고
    • Cell transformation by the superoxide-generating oxidase Mox1
    • Suh YA, Arnold RS, Lassegue B, Shi J, Xu X, et al. (1999) Cell transformation by the superoxide-generating oxidase Mox1. Nature 401: 79-82.
    • (1999) Nature , vol.401 , pp. 79-82
    • Suh, Y.A.1    Arnold, R.S.2    Lassegue, B.3    Shi, J.4    Xu, X.5
  • 12
    • 0035897653 scopus 로고    scopus 로고
    • Homologs of gp91phox: Cloning and tissue expression of Nox3, Nox4, and Nox5
    • Cheng G, Cao Z, Xu X, van Meir EG, Lambeth JD (2001) Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5. Gene 269: 131-140.
    • (2001) Gene , vol.269 , pp. 131-140
    • Cheng, G.1    Cao, Z.2    Xu, X.3    van Meir, E.G.4    Lambeth, J.D.5
  • 14
    • 0035813159 scopus 로고    scopus 로고
    • A Ca(2+)- activated NADPH oxidase in testis, spleen, and lymph nodes
    • Banfi B, Molnar G, Maturana A, Steger K, Hegedus B, et al. (2001) A Ca(2+)- activated NADPH oxidase in testis, spleen, and lymph nodes. J Biol Chem 276: 37594-37601.
    • (2001) J Biol Chem , vol.276 , pp. 37594-37601
    • Banfi, B.1    Molnar, G.2    Maturana, A.3    Steger, K.4    Hegedus, B.5
  • 15
    • 0036134932 scopus 로고    scopus 로고
    • Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases
    • Lambeth JD (2002) Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases. Curr Opin Hematol 9: 11-17.
    • (2002) Curr Opin Hematol , vol.9 , pp. 11-17
    • Lambeth, J.D.1
  • 16
    • 0347711117 scopus 로고    scopus 로고
    • NADPH oxidases: Not just for leukocytes anymore!
    • Bokoch GM, Knaus UG (2003) NADPH oxidases: not just for leukocytes anymore! Trends Biochem Sci 28: 502-508.
    • (2003) Trends Biochem Sci , vol.28 , pp. 502-508
    • Bokoch, G.M.1    Knaus, U.G.2
  • 17
    • 9644259382 scopus 로고    scopus 로고
    • The role of phosphoinositides and phosphorylation in regulation of NADPH oxidase
    • Perisic O, Wilson MI, Karathanassis D, Bravo J, Pacold ME, et al. (2004) The role of phosphoinositides and phosphorylation in regulation of NADPH oxidase. Adv Enzyme Regul 44: 279-298.
    • (2004) Adv Enzyme Regul , vol.44 , pp. 279-298
    • Perisic, O.1    Wilson, M.I.2    Karathanassis, D.3    Bravo, J.4    Pacold, M.E.5
  • 18
    • 15944372262 scopus 로고    scopus 로고
    • Activation and assembly of the NADPH oxidase: A structural perspective
    • Groemping Y, Rittinger K (2005) Activation and assembly of the NADPH oxidase: a structural perspective. Biochem J 386: 401-416.
    • (2005) Biochem J , vol.386 , pp. 401-416
    • Groemping, Y.1    Rittinger, K.2
  • 19
    • 0028142461 scopus 로고
    • The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases
    • El Benna J, Faust LP, Babior BM (1994) The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases. J Biol Chem 269: 23431-23436.
    • (1994) J Biol Chem , vol.269 , pp. 23431-23436
    • El Benna, J.1    Faust, L.P.2    Babior, B.M.3
  • 20
    • 0027973549 scopus 로고
    • Assembly of the phagocyte NADPH oxidase: Binding of Src homology 3 domains to proline-rich targets
    • Leto TL, Adams AG, de Mendez I (1994) Assembly of the phagocyte NADPH oxidase: binding of Src homology 3 domains to proline-rich targets. Proc Natl Acad Sci U S A 91: 10650-10654.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10650-10654
    • Leto, T.L.1    Adams, A.G.2    de Mendez, I.3
  • 21
    • 0033585122 scopus 로고    scopus 로고
    • Mechanism for phosphorylationinduced activation of the phagocyte NADPH oxidase protein p47(phox). Triple replacement of serines 303, 304, and 328 with aspartates disrupts the SH3 domain-mediated intramolecular interaction in p47(phox), thereby activating the oxidase
    • Ago T, Nunoi H, Ito T, Sumimoto H (1999) Mechanism for phosphorylationinduced activation of the phagocyte NADPH oxidase protein p47(phox). Triple replacement of serines 303, 304, and 328 with aspartates disrupts the SH3 domain-mediated intramolecular interaction in p47(phox), thereby activating the oxidase. J Biol Chem 274: 33644-33653.
    • (1999) J Biol Chem , vol.274 , pp. 33644-33653
    • Ago, T.1    Nunoi, H.2    Ito, T.3    Sumimoto, H.4
  • 22
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylation-induced activation of the NADPH oxidase
    • Groemping Y, Lapouge K, Smerdon SJ, 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
  • 23
    • 0033538550 scopus 로고    scopus 로고
    • Activation of the phagocyte NADPH oxidase protein p47(phox). Phosphorylation controls SH3 domain-dependent binding to p22(phox)
    • Huang J, Kleinberg ME (1999) Activation of the phagocyte NADPH oxidase protein p47(phox). Phosphorylation controls SH3 domain-dependent binding to p22(phox). J Biol Chem 274: 19731-19737.
    • (1999) J Biol Chem , vol.274 , pp. 19731-19737
    • Huang, J.1    Kleinberg, M.E.2
  • 24
    • 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 NN, Fujioka Y, Ogura K, Sumimoto H, et al. (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
  • 25
    • 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
  • 26
    • 0037155889 scopus 로고    scopus 로고
    • Architecture of the p40- p47-p67phox complex in the resting state of the NADPH oxidase. A central role for p67phox
    • Lapouge K, Smith SJ, Groemping Y, Rittinger K (2002) Architecture of the p40- p47-p67phox complex in the resting state of the NADPH oxidase. A central role for p67phox. J Biol Chem 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
  • 27
    • 17144412976 scopus 로고    scopus 로고
    • Effects of p47phox C terminus phosphorylations on binding interactions with p40phox and p67phox. Structural and functional comparison of p40phox and p67phox SH3 domains
    • Massenet C, Chenavas S, Cohen-Addad C, Dagher MC, Brandolin G, et al. (2005) Effects of p47phox C terminus phosphorylations on binding interactions with p40phox and p67phox. Structural and functional comparison of p40phox and p67phox SH3 domains. J Biol Chem 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
  • 28
    • 0038205912 scopus 로고    scopus 로고
    • NAD(P)H oxidase 1, a product of differentiated colon epithelial cells, can partially replace glycoprotein 91phox in the regulated production of superoxide by phagocytes
    • Geiszt M, Lekstrom K, Brenner S, Hewitt SM, Dana R, et al. (2003) NAD(P)H oxidase 1, a product of differentiated colon epithelial cells, can partially replace glycoprotein 91phox in the regulated production of superoxide by phagocytes. J Immunol 171: 299-306.
    • (2003) J Immunol , vol.171 , pp. 299-306
    • Geiszt, M.1    Lekstrom, K.2    Brenner, S.3    Hewitt, S.M.4    Dana, R.5
  • 29
    • 1342324604 scopus 로고    scopus 로고
    • Role of nicotinamide adenine dinucleotide phosphate oxidase 1 in oxidative burst response to Toll-like receptor 5 signaling in large intestinal epithelial cells
    • Kawahara T, Kuwano Y, Teshima-Kondo S, Takeya R, Sumimoto H, et al. (2004) Role of nicotinamide adenine dinucleotide phosphate oxidase 1 in oxidative burst response to Toll-like receptor 5 signaling in large intestinal epithelial cells. J Immunol 172: 3051-3058.
    • (2004) J Immunol , vol.172 , pp. 3051-3058
    • Kawahara, T.1    Kuwano, Y.2    Teshima-Kondo, S.3    Takeya, R.4    Sumimoto, H.5
  • 30
    • 0035826733 scopus 로고    scopus 로고
    • Hydrogen peroxide mediates the cell growth and transformation caused by the mitogenic oxidase Nox1
    • Arnold RS, Shi J, Murad E, Whalen AM, Sun CQ, et al. (2001) Hydrogen peroxide mediates the cell growth and transformation caused by the mitogenic oxidase Nox1. Proc Natl Acad Sci U S A 98: 5550-5555.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 5550-5555
    • Arnold, R.S.1    Shi, J.2    Murad, E.3    Whalen, A.M.4    Sun, C.Q.5
  • 31
    • 33750912209 scopus 로고    scopus 로고
    • NADPH oxidases in the gastrointestinal tract: A potential role of Nox1 in innate immune response and carcinogenesis
    • Rokutan K, Kawahara T, Kuwano Y, Tominaga K, Sekiyama A, et al. (2006) NADPH oxidases in the gastrointestinal tract: a potential role of Nox1 in innate immune response and carcinogenesis. Antioxid Redox Signal 8: 1573-1582.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1573-1582
    • Rokutan, K.1    Kawahara, T.2    Kuwano, Y.3    Tominaga, K.4    Sekiyama, A.5
  • 32
    • 0038036799 scopus 로고    scopus 로고
    • Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells
    • Geiszt M, Lekstrom K, Witta J, Leto TL (2003) Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells. J Biol Chem 278: 20006-20012.
    • (2003) J Biol Chem , vol.278 , pp. 20006-20012
    • Geiszt, M.1    Lekstrom, K.2    Witta, J.3    Leto, T.L.4
  • 33
    • 0038789165 scopus 로고    scopus 로고
    • Two novel proteins activate superoxide generation by the NADPH oxidase NOX1
    • Banfi B, Clark RA, Steger K, Krause KH (2003) Two novel proteins activate superoxide generation by the NADPH oxidase NOX1. J Biol Chem 278: 3510-3513.
    • (2003) J Biol Chem , vol.278 , pp. 3510-3513
    • Banfi, B.1    Clark, R.A.2    Steger, K.3    Krause, K.H.4
  • 34
    • 0042991381 scopus 로고    scopus 로고
    • Novel human homologues of p47phox and p67phox participate in activation of superoxideproducing NADPH oxidases
    • Takeya R, Ueno N, Kami K, Taura M, Kohjima M, et al. (2003) Novel human homologues of p47phox and p67phox participate in activation of superoxideproducing NADPH oxidases. J Biol Chem 278: 25234-25246.
    • (2003) J Biol Chem , vol.278 , pp. 25234-25246
    • Takeya, R.1    Ueno, N.2    Kami, K.3    Taura, M.4    Kohjima, M.5
  • 35
    • 33644750712 scopus 로고    scopus 로고
    • Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-based NADPH oxidases
    • Ueyama T, Geiszt M, Leto TL (2006) Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-based NADPH oxidases. Mol Cell Biol 26: 2160-2174.
    • (2006) Mol Cell Biol , vol.26 , pp. 2160-2174
    • Ueyama, T.1    Geiszt, M.2    Leto, T.L.3
  • 37
    • 36849064316 scopus 로고    scopus 로고
    • Molecular evolution of Phox-related regulatory subunits for NADPH oxidase enzymes
    • Kawahara T, Lambeth JD (2007) Molecular evolution of Phox-related regulatory subunits for NADPH oxidase enzymes. BMC Evol Biol 7: 178.
    • (2007) BMC Evol Biol , vol.7 , pp. 178
    • Kawahara, T.1    Lambeth, J.D.2
  • 38
    • 1042289744 scopus 로고    scopus 로고
    • NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain
    • Cheng G, Lambeth JD (2004) NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain. J Biol Chem 279: 4737-4742.
    • (2004) J Biol Chem , vol.279 , pp. 4737-4742
    • Cheng, G.1    Lambeth, J.D.2
  • 39
    • 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
  • 40
    • 33751512270 scopus 로고    scopus 로고
    • Interaction between the SH3 domains and C-terminal proline-rich region in NADPH oxidase organizer 1 (Noxo1)
    • Yamamoto A, Kami K, Takeya R, Sumimoto H (2007) Interaction between the SH3 domains and C-terminal proline-rich region in NADPH oxidase organizer 1 (Noxo1). Biochem Biophys Res Commun 352: 560-565.
    • (2007) Biochem Biophys Res Commun , vol.352 , pp. 560-565
    • Yamamoto, A.1    Kami, K.2    Takeya, R.3    Sumimoto, H.4
  • 42
    • 18744383603 scopus 로고    scopus 로고
    • Topography for independent binding of alpha-helical and PPII-helical ligands to a peroxisomal SH3 domain
    • Douangamath A, Filipp FV, Klein AT, Barnett P, Zou P, et al. (2002) Topography for independent binding of alpha-helical and PPII-helical ligands to a peroxisomal SH3 domain. Mol Cell 10: 1007-1017.
    • (2002) Mol Cell , vol.10 , pp. 1007-1017
    • Douangamath, A.1    Filipp, F.V.2    Klein, A.T.3    Barnett, P.4    Zou, P.5
  • 43
    • 0033579491 scopus 로고    scopus 로고
    • A phosphatidic acidactivated protein kinase and conventional protein kinase C isoforms phosphorylate p22(phox), an NADPH oxidase component
    • Regier DS, Waite KA, Wallin R, McPhail LC (1999) A phosphatidic acidactivated protein kinase and conventional protein kinase C isoforms phosphorylate p22(phox), an NADPH oxidase component. J Biol Chem 274: 36601-36608.
    • (1999) J Biol Chem , vol.274 , pp. 36601-36608
    • Regier, D.S.1    Waite, K.A.2    Wallin, R.3    McPhail, L.C.4
  • 44
    • 0034664253 scopus 로고    scopus 로고
    • Phosphorylation of p22phox is mediated by phospholipase D-dependent and - independent mechanisms. Correlation of NADPH oxidase activity and p22phox phosphorylation
    • Regier DS, Greene DG, Sergeant S, Jesaitis AJ, McPhail LC (2000) Phosphorylation of p22phox is mediated by phospholipase D-dependent and - independent mechanisms. Correlation of NADPH oxidase activity and p22phox phosphorylation. J Biol Chem 275: 28406-28412.
    • (2000) J Biol Chem , vol.275 , pp. 28406-28412
    • Regier, D.S.1    Greene, D.G.2    Sergeant, S.3    Jesaitis, A.J.4    McPhail, L.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.