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Volumn 280, Issue 20, 2013, Pages 5145-5159

Phosphorylation of Noxo1 at threonine 341 regulates its interaction with Noxa1 and the superoxide-producing activity of Nox1

Author keywords

NADPH oxidase; Nox1; Noxa1; Noxo1; protein kinase A; protein kinase C

Indexed keywords

2 [1 (3 DIMETHYLAMINOPROPYL) 3 INDOLYL] 3 (3 INDOLYL)MALEIMIDE; ALANINE; COMPLEMENTARY DNA; CYCLIC AMP DEPENDENT PROTEIN KINASE; NOX ACTIVATOR 1; NOX ORGANIZER 1; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; REGULATOR PROTEIN; SUPEROXIDE; THREONINE; UNCLASSIFIED DRUG;

EID: 84885306566     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12489     Document Type: Article
Times cited : (30)

References (43)
  • 1
    • 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
  • 2
    • 33745804975 scopus 로고    scopus 로고
    • The expanding role of NADPH oxidases in health and disease: No longer just agents of death and destruction
    • Quinn MT, Ammons MC, &, Deleo FR, (2006) The expanding role of NADPH oxidases in health and disease: no longer just agents of death and destruction. Clin Sci (London) 111, 1-20.
    • (2006) Clin Sci (London) , vol.111 , pp. 1-20
    • Quinn, M.T.1    Ammons, M.C.2    Deleo, F.R.3
  • 3
    • 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
  • 4
    • 44949106317 scopus 로고    scopus 로고
    • Structure, regulation and evolution of Nox-family NADPH oxidases that produce reactive oxygen species
    • Sumimoto H, (2008) Structure, regulation and evolution of Nox-family NADPH oxidases that produce reactive oxygen species. FEBS J 275, 3249-3277.
    • (2008) FEBS J , vol.275 , pp. 3249-3277
    • Sumimoto, H.1
  • 5
    • 77949593677 scopus 로고    scopus 로고
    • Targeting and regulation of reactive oxygen species generation by Nox family NADPH oxidases
    • Leto TL, Morand S, Hurt D, &, Ueyama T, (2009) Targeting and regulation of reactive oxygen species generation by Nox family NADPH oxidases. Antioxid Redox Signal 11, 2607-2619.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2607-2619
    • Leto, T.L.1    Morand, S.2    Hurt, D.3    Ueyama, T.4
  • 7
    • 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
  • 9
    • 0034607649 scopus 로고    scopus 로고
    • phox to activate the phagocyte NADPH oxidase
    • phox to activate the phagocyte NADPH oxidase. J Biol Chem 275, 13793-13801.
    • (2000) J Biol Chem , vol.275 , pp. 13793-13801
    • Shiose, A.1    Sumimoto, H.2
  • 10
    • 0028142461 scopus 로고
    • phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases
    • phox 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
  • 15
    • 79957890939 scopus 로고    scopus 로고
    • Combating oxidative stress in vascular disease: NADPH oxidases as therapeutic targets
    • Drummond GR, Selemidis S, Griendling KK, &, Sobey CG, (2011) Combating oxidative stress in vascular disease: NADPH oxidases as therapeutic targets. Nat Rev Drug Discov 10, 453-471.
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 453-471
    • Drummond, G.R.1    Selemidis, S.2    Griendling, K.K.3    Sobey, C.G.4
  • 16
    • 84861062943 scopus 로고    scopus 로고
    • Biochemistry, physiology, and pathophysiology of NADPH oxidases in the cardiovascular system
    • Lassègue B, San Martín A, &, Griendling KK, (2012) Biochemistry, physiology, and pathophysiology of NADPH oxidases in the cardiovascular system. Circ Res 110, 1364-1390.
    • (2012) Circ Res , vol.110 , pp. 1364-1390
    • Lassègue, B.1    San Martín, A.2    Griendling, K.K.3
  • 18
    • 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 RK, Kumar P, Griendling KK, Schmidt HH, Busse R, &, Brandes RP, (2004) Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase. J Biol Chem 279, 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
  • 19
    • 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, &, Sumimoto H, (2006) Direct involvement of the small GTPase Rac in activation of the superoxide-producing NADPH oxidase Nox1. J Biol Chem 281, 21857-21868.
    • (2006) J Biol Chem , vol.281 , pp. 21857-21868
    • Miyano, K.1    Ueno, N.2    Takeya, R.3    Sumimoto, H.4
  • 20
    • 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, 20006-20012.
    • (2003) J Biol Chem , vol.278 , pp. 20006-20012
    • Geiszt, M.1    Lekstrom, K.2    Witta, J.3    Leto, T.L.4
  • 21
    • 0038789165 scopus 로고    scopus 로고
    • Two novel proteins activate superoxide generation by the NADPH oxidase NOX1
    • Bánfi 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
    • Bánfi, B.1    Clark, R.A.2    Steger, K.3    Krause, K.H.4
  • 22
    • 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
  • 23
    • 33745815084 scopus 로고    scopus 로고
    • Nox1-dependent reactive oxygen generation is regulated by Rac1
    • Cheng G, Diebold BA, Hughes Y, &, Lambeth JD, (2006) Nox1-dependent reactive oxygen generation is regulated by Rac1. J Biol Chem 281, 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
  • 24
    • 34547852395 scopus 로고    scopus 로고
    • phox-dependent NADPH oxidases
    • phox-dependent NADPH oxidases. Biochimie 89, 1133-1144.
    • (2007) Biochimie , vol.89 , pp. 1133-1144
    • Miyano, K.1    Sumimoto, H.2
  • 25
    • 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
  • 26
    • 33746779417 scopus 로고    scopus 로고
    • Expression and function of Noxo1γ, an alternative splicing form of the NADPH oxidase organizer 1
    • Takeya R, Taura M, Yamasaki T, Naito S, &, Sumimoto H, (2006) Expression and function of Noxo1γ, an alternative splicing form of the NADPH oxidase organizer 1. FEBS J 273, 3663-3677.
    • (2006) FEBS J , vol.273 , pp. 3663-3677
    • Takeya, R.1    Taura, M.2    Yamasaki, T.3    Naito, S.4    Sumimoto, H.5
  • 28
    • 67849088501 scopus 로고    scopus 로고
    • Importance of NOX1 for angiotensin II-induced cerebrovascular superoxide production and cortical infarct volume following ischemic stroke
    • Jackman KA, Miller AA, Drummond GR, &, Sobey CG, (2009) Importance of NOX1 for angiotensin II-induced cerebrovascular superoxide production and cortical infarct volume following ischemic stroke. Brain Res 1286, 215-220.
    • (2009) Brain Res , vol.1286 , pp. 215-220
    • Jackman, K.A.1    Miller, A.A.2    Drummond, G.R.3    Sobey, C.G.4
  • 30
    • 38049173243 scopus 로고    scopus 로고
    • Mechanism of angiotensin II-induced superoxide production in cells reconstituted with angiotensin type 1 receptor and the components of NADPH oxidase
    • Choi H, Leto TL, Hunyady L, Catt KJ, Bae YS, &, Rhee SG, (2008) Mechanism of angiotensin II-induced superoxide production in cells reconstituted with angiotensin type 1 receptor and the components of NADPH oxidase. J Biol Chem 283, 255-267.
    • (2008) J Biol Chem , vol.283 , pp. 255-267
    • Choi, H.1    Leto, T.L.2    Hunyady, L.3    Catt, K.J.4    Bae, Y.S.5    Rhee, S.G.6
  • 31
    • 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
  • 33
    • 36849030223 scopus 로고    scopus 로고
    • Regulation of Nox1 activity via protein kinase A-mediated phosphorylation of NoxA1 and 14-3-3 binding
    • Kim JS, Diebold BA, Babior BM, Knaus UG, &, Bokoch GM, (2007) Regulation of Nox1 activity via protein kinase A-mediated phosphorylation of NoxA1 and 14-3-3 binding. J Biol Chem 282, 34787-34800.
    • (2007) J Biol Chem , vol.282 , pp. 34787-34800
    • Kim, J.S.1    Diebold, B.A.2    Babior, B.M.3    Knaus, U.G.4    Bokoch, G.M.5
  • 34
    • 77950517955 scopus 로고    scopus 로고
    • Phosphorylation of serine282 in NADPH oxidase activator 1 by Erk desensitizes EGF-induced ROS generation
    • Oh H, Jung HY, Kim J, &, Bae YS, (2010) Phosphorylation of serine282 in NADPH oxidase activator 1 by Erk desensitizes EGF-induced ROS generation. Biochem Biophys Res Commun 394, 691-696.
    • (2010) Biochem Biophys Res Commun , vol.394 , pp. 691-696
    • Oh, H.1    Jung, H.Y.2    Kim, J.3    Bae, Y.S.4
  • 35
    • 77953526221 scopus 로고    scopus 로고
    • Phosphorylation of NADPH oxidase activator 1 (NOXA1) on serine 282 by MAP kinases and on serine 172 by protein kinase C and protein kinase A prevents NOX1 hyperactivation
    • Kroviarski Y, Debbabi M, Bachoual R, Perianin A, Gougerot-Pocidalo MA, El-Benna J, &, Dang PM, (2010) Phosphorylation of NADPH oxidase activator 1 (NOXA1) on serine 282 by MAP kinases and on serine 172 by protein kinase C and protein kinase A prevents NOX1 hyperactivation. FASEB J 24, 2077-2092.
    • (2010) FASEB J , vol.24 , pp. 2077-2092
    • Kroviarski, Y.1    Debbabi, M.2    Bachoual, R.3    Perianin, A.4    Gougerot-Pocidalo, M.A.5    El-Benna, J.6    Dang, P.M.7
  • 36
    • 0033580822 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase-dependent and -independent activation of the small GTPase Rac2 in human neutrophils
    • Akasaki T, Koga H, &, Sumimoto H, (1999) Phosphoinositide 3-kinase-dependent and -independent activation of the small GTPase Rac2 in human neutrophils. J Biol Chem 274, 18055-18059.
    • (1999) J Biol Chem , vol.274 , pp. 18055-18059
    • Akasaki, T.1    Koga, H.2    Sumimoto, H.3
  • 38
    • 84875732742 scopus 로고    scopus 로고
    • NOXO1 phosphorylation on serine 154 is critical for optimal NADPH oxidase 1 assembly and activation
    • Debbabi M, Kroviarski Y, Bournier O, Gougerot-Pocidalo MA, El-Benna J, &, Dang PM, (2013) NOXO1 phosphorylation on serine 154 is critical for optimal NADPH oxidase 1 assembly and activation. FASEB J 27, 1733-1748.
    • (2013) FASEB J , vol.27 , pp. 1733-1748
    • Debbabi, M.1    Kroviarski, Y.2    Bournier, O.3    Gougerot-Pocidalo, M.A.4    El-Benna, J.5    Dang, P.M.6
  • 40
    • 0024991898 scopus 로고
    • PEF-BOS, a powerful mammalian expression vector
    • Mizushima S, &, Nagata S, (1990) pEF-BOS, a powerful mammalian expression vector. Nucleic Acids Res 18, 5322.
    • (1990) Nucleic Acids Res , vol.18 , pp. 5322
    • Mizushima, S.1    Nagata, S.2
  • 42
    • 0032237775 scopus 로고    scopus 로고
    • Fragmentation of phosphopeptides in an ion trap mass spectrometer
    • DeGnore JP, &, Qin J, (1998) Fragmentation of phosphopeptides in an ion trap mass spectrometer. J Am Soc Mass Spectrom 9, 1175-1188.
    • (1998) J Am Soc Mass Spectrom , vol.9 , pp. 1175-1188
    • Degnore, J.P.1    Qin, J.2
  • 43
    • 0025688754 scopus 로고
    • Liquid secondary ion mass spectrometry of phosphorylated and sulfated peptides and proteins
    • Gibson BW, &, Cohen P, (1990) Liquid secondary ion mass spectrometry of phosphorylated and sulfated peptides and proteins. Methods Enzymol 193, 480-501.
    • (1990) Methods Enzymol , vol.193 , pp. 480-501
    • Gibson, B.W.1    Cohen, P.2


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