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Volumn 588, Issue 17, 2014, Pages 2837-2843

Phosphorylation of flotillin-1 by mitochondrial c-Src is required to prevent the production of reactive oxygen species

Author keywords

c Src; Mitochondria; Protein phosphorylation; Reactive oxygen species; Respiratory complex; Tyrosine kinase

Indexed keywords

4 AMINO 7 TERT BUTYL 5 (4 CHLOROPHENYL)PYRAZOLO[3,4 D]PYRIMIDINE; CYTOCHROME; FLOTILLIN 1; MUTANT PROTEIN; REACTIVE OXYGEN METABOLITE; RESPIRATORY COMPLEX II; TYROSINE; UNCLASSIFIED DRUG;

EID: 84907821817     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.06.044     Document Type: Article
Times cited : (16)

References (48)
  • 1
    • 34247383227 scopus 로고    scopus 로고
    • Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS
    • J. Lee, Y. Xu, Y. Chen, R. Sprung, S.C. Kim, S. Xie, and Y. Zhao Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS Mol. Cell. Proteomics 6 2007 669 676
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 669-676
    • Lee, J.1    Xu, Y.2    Chen, Y.3    Sprung, R.4    Kim, S.C.5    Xie, S.6    Zhao, Y.7
  • 3
    • 18044384816 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in mitochondria: A new frontier in mitochondrial signaling
    • M. Salvi, A.M. Brunati, and A. Toninello Tyrosine phosphorylation in mitochondria: a new frontier in mitochondrial signaling Free Radic. Biol. Med. 38 2005 1267 1277
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1267-1277
    • Salvi, M.1    Brunati, A.M.2    Toninello, A.3
  • 4
    • 84870695545 scopus 로고    scopus 로고
    • Src kinases are important regulators of mitochondrial functions
    • E. Hebert-Chatelain Src kinases are important regulators of mitochondrial functions Int. J. Biochem. Cell Biol. 45 2012 90 98
    • (2012) Int. J. Biochem. Cell Biol. , vol.45 , pp. 90-98
    • Hebert-Chatelain, E.1
  • 5
    • 0037416134 scopus 로고    scopus 로고
    • Regulation of cytochrome c oxidase activity by c-Src in osteoclasts
    • T. Miyazaki, L. Neff, S. Tanaka, W.C. Horne, and R. Baron Regulation of cytochrome c oxidase activity by c-Src in osteoclasts J. Cell Biol. 160 2003 709 718
    • (2003) J. Cell Biol. , vol.160 , pp. 709-718
    • Miyazaki, T.1    Neff, L.2    Tanaka, S.3    Horne, W.C.4    Baron, R.5
  • 9
    • 84866880855 scopus 로고    scopus 로고
    • Mitochondrial c-Src regulates cell survival through phosphorylation of respiratory chain components
    • M. Ogura, J. Yamaki, M.K. Homma, and Y. Homma Mitochondrial c-Src regulates cell survival through phosphorylation of respiratory chain components Biochem. J. 447 2012 281 289
    • (2012) Biochem. J. , vol.447 , pp. 281-289
    • Ogura, M.1    Yamaki, J.2    Homma, M.K.3    Homma, Y.4
  • 10
    • 22544453858 scopus 로고    scopus 로고
    • Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth
    • E. Giannoni, F. Buricchi, G. Raugei, G. Ramponi, and P. Chiarugi Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth Mol. Cell. Biol. 25 2005 6391 6403
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6391-6403
    • Giannoni, E.1    Buricchi, F.2    Raugei, G.3    Ramponi, G.4    Chiarugi, P.5
  • 11
    • 65249173530 scopus 로고    scopus 로고
    • Direct and specific inactivation of protein tyrosine kinases in the Src and FGFR families by reversible cysteine oxidation
    • D.J. Kemble, and G. Sun Direct and specific inactivation of protein tyrosine kinases in the Src and FGFR families by reversible cysteine oxidation Proc. Natl. Acad. Sci. USA 106 2009 5070 5075
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5070-5075
    • Kemble, D.J.1    Sun, G.2
  • 13
    • 84887420291 scopus 로고    scopus 로고
    • Myotonic dystrophy protein kinase (DMPK) prevents ROS-induced cell death by assembling a hexokinase II-Src complex on the mitochondrial surface
    • B. Pantic, E. Trevisan, A. Citta, M.P. Rigobello, O. Marin, P. Bernardi, S. Salvatori, and A. Rasola Myotonic dystrophy protein kinase (DMPK) prevents ROS-induced cell death by assembling a hexokinase II-Src complex on the mitochondrial surface Cell Death Dis. 4 2013 e858
    • (2013) Cell Death Dis. , vol.4 , pp. 858
    • Pantic, B.1    Trevisan, E.2    Citta, A.3    Rigobello, M.P.4    Marin, O.5    Bernardi, P.6    Salvatori, S.7    Rasola, A.8
  • 14
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • M.P. Murphy How mitochondria produce reactive oxygen species Biochem. J. 417 2009 1 13
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 15
    • 67650248980 scopus 로고    scopus 로고
    • Oxygen sensitivity of mitochondrial reactive oxygen species generation depends on metabolic conditions
    • D.L. Hoffman, and P.S. Brookes Oxygen sensitivity of mitochondrial reactive oxygen species generation depends on metabolic conditions J. Biol. Chem. 284 2009 16236 16245
    • (2009) J. Biol. Chem. , vol.284 , pp. 16236-16245
    • Hoffman, D.L.1    Brookes, P.S.2
  • 17
    • 70350351403 scopus 로고    scopus 로고
    • Structural basis for the mechanism of respiratory complex i
    • J.M. Berrisford, and L.A. Sazanov Structural basis for the mechanism of respiratory complex I J. Biol. Chem. 284 2009 29773 29783
    • (2009) J. Biol. Chem. , vol.284 , pp. 29773-29783
    • Berrisford, J.M.1    Sazanov, L.A.2
  • 20
    • 79960584575 scopus 로고    scopus 로고
    • Mitochondrial complex II has a key role in mitochondrial-derived reactive oxygen species influence on plant stress gene regulation and defense
    • C. Gleason, S. Huang, L.F. Thatcher, R.C. Foley, C.R. Anderson, A.J. Carroll, A.H. Millar, and K.B. Singh Mitochondrial complex II has a key role in mitochondrial-derived reactive oxygen species influence on plant stress gene regulation and defense Proc. Natl. Acad. Sci. USA 108 2011 10768 10773
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 10768-10773
    • Gleason, C.1    Huang, S.2    Thatcher, L.F.3    Foley, R.C.4    Anderson, C.R.5    Carroll, A.J.6    Millar, A.H.7    Singh, K.B.8
  • 21
    • 78651282654 scopus 로고    scopus 로고
    • Specific disintegration of complex II succinate: Ubiquinone oxidoreductase links pH changes to oxidative stress for apoptosis induction
    • A. Lemarie, L. Huc, E. Pazarentzos, A.L. Mahul-Mellier, and S. Grimm Specific disintegration of complex II succinate: ubiquinone oxidoreductase links pH changes to oxidative stress for apoptosis induction Cell Death Differ. 18 2011 338 349
    • (2011) Cell Death Differ. , vol.18 , pp. 338-349
    • Lemarie, A.1    Huc, L.2    Pazarentzos, E.3    Mahul-Mellier, A.L.4    Grimm, S.5
  • 22
    • 84864540083 scopus 로고    scopus 로고
    • Mitochondrial complex II can generate reactive oxygen species at high rates in both the forward and reverse reactions
    • C.L. Quinlan, A.L. Orr, I.V. Perevoshchikova, J.R. Treberg, B.A. Ackrell, and M.D. Brand Mitochondrial complex II can generate reactive oxygen species at high rates in both the forward and reverse reactions J. Biol. Chem. 287 2012 27255 27264
    • (2012) J. Biol. Chem. , vol.287 , pp. 27255-27264
    • Quinlan, C.L.1    Orr, A.L.2    Perevoshchikova, I.V.3    Treberg, J.R.4    Ackrell, B.A.5    Brand, M.D.6
  • 23
    • 84866625277 scopus 로고    scopus 로고
    • A disintegrin and metalloproteinase 15 contributes to atherosclerosis by mediating endothelial barrier dysfunction via Src family kinase activity
    • C. Sun, M.H. Wu, E.S. Lee, and S.Y. Yuan A disintegrin and metalloproteinase 15 contributes to atherosclerosis by mediating endothelial barrier dysfunction via Src family kinase activity Arterioscler. Thromb. Vasc. Biol. 32 2012 2444 2451
    • (2012) Arterioscler. Thromb. Vasc. Biol. , vol.32 , pp. 2444-2451
    • Sun, C.1    Wu, M.H.2    Lee, E.S.3    Yuan, S.Y.4
  • 25
    • 0036319021 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the mitochondrial electron transport chain
    • Y. Liu, G. Fiskum, and D. Schubert Generation of reactive oxygen species by the mitochondrial electron transport chain J. Neurochem. 80 2002 780 787
    • (2002) J. Neurochem. , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 27
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • A. Boveris, N. Oshino, and B. Chance The cellular production of hydrogen peroxide Biochem. J. 128 1972 617 630
    • (1972) Biochem. J. , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 33
    • 84866665390 scopus 로고    scopus 로고
    • Mitochondria and cancer
    • D.C. Wallace Mitochondria and cancer Nat. Rev. Cancer 12 2012 685 698
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 685-698
    • Wallace, D.C.1
  • 34
    • 50649095537 scopus 로고    scopus 로고
    • Reactive oxygen species act remotely to cause synapse loss in a Drosophila model of developmental mitochondrial encephalopathy
    • J.D. Mast, K.M. Tomalty, H. Vogel, and T.R. Clandinin Reactive oxygen species act remotely to cause synapse loss in a Drosophila model of developmental mitochondrial encephalopathy Development 135 2008 2669 2679
    • (2008) Development , vol.135 , pp. 2669-2679
    • Mast, J.D.1    Tomalty, K.M.2    Vogel, H.3    Clandinin, T.R.4
  • 35
    • 21244503033 scopus 로고    scopus 로고
    • Crystal structure of mitochondrial respiratory membrane protein complex II
    • F. Sun, X. Huo, Y. Zhai, A. Wang, J. Xu, D. Su, M. Bartlam, and Z. Rao Crystal structure of mitochondrial respiratory membrane protein complex II Cell 121 2005 1043 1057
    • (2005) Cell , vol.121 , pp. 1043-1057
    • Sun, F.1    Huo, X.2    Zhai, Y.3    Wang, A.4    Xu, J.5    Su, D.6    Bartlam, M.7    Rao, Z.8
  • 38
    • 78349264648 scopus 로고    scopus 로고
    • Flotillin microdomains interact with the cortical cytoskeleton to control uropod formation and neutrophil recruitment
    • A. Ludwig, G.P. Otto, K. Riento, E. Hams, P.G. Fallon, and B.J. Nichols Flotillin microdomains interact with the cortical cytoskeleton to control uropod formation and neutrophil recruitment J. Cell Biol. 191 2010 771 781
    • (2010) J. Cell Biol. , vol.191 , pp. 771-781
    • Ludwig, A.1    Otto, G.P.2    Riento, K.3    Hams, E.4    Fallon, P.G.5    Nichols, B.J.6
  • 39
    • 79956033520 scopus 로고    scopus 로고
    • Knockdown of FLOT1 impairs cell proliferation and tumorigenicity in breast cancer through upregulation of FOXO3a
    • C. Lin, Z. Wu, X. Lin, C. Yu, T. Shi, Y. Zeng, X. Wang, J. Li, and L. Song Knockdown of FLOT1 impairs cell proliferation and tumorigenicity in breast cancer through upregulation of FOXO3a Clin. Cancer Res. 17 2011 3089 3099
    • (2011) Clin. Cancer Res. , vol.17 , pp. 3089-3099
    • Lin, C.1    Wu, Z.2    Lin, X.3    Yu, C.4    Shi, T.5    Zeng, Y.6    Wang, X.7    Li, J.8    Song, L.9
  • 40
    • 84857746692 scopus 로고    scopus 로고
    • Flotillin-1/reggie-2 protein plays dual role in activation of receptor-tyrosine kinase/mitogen-activated protein kinase signaling
    • M. Amaddii, M. Meister, A. Banning, A. Tomasovic, J. Mooz, K. Rajalingam, and R. Tikkanen Flotillin-1/reggie-2 protein plays dual role in activation of receptor-tyrosine kinase/mitogen-activated protein kinase signaling J. Biol. Chem. 287 2012 7265 7278
    • (2012) J. Biol. Chem. , vol.287 , pp. 7265-7278
    • Amaddii, M.1    Meister, M.2    Banning, A.3    Tomasovic, A.4    Mooz, J.5    Rajalingam, K.6    Tikkanen, R.7
  • 43
    • 66849106387 scopus 로고    scopus 로고
    • Endocytosis of flotillin-1 and flotillin-2 is regulated by Fyn kinase
    • K. Riento, M. Frick, I. Schafer, and B.J. Nichols Endocytosis of flotillin-1 and flotillin-2 is regulated by Fyn kinase J. Cell Sci. 122 2009 912 918
    • (2009) J. Cell Sci. , vol.122 , pp. 912-918
    • Riento, K.1    Frick, M.2    Schafer, I.3    Nichols, B.J.4
  • 46
    • 67349189783 scopus 로고    scopus 로고
    • Hetero-oligomerization of reggie-1/flotillin-2 and reggie-2/flotillin-1 is required for their endocytosis
    • T. Babuke, M. Ruonala, M. Meister, M. Amaddii, C. Genzler, A. Esposito, and R. Tikkanen Hetero-oligomerization of reggie-1/flotillin-2 and reggie-2/flotillin-1 is required for their endocytosis Cell. Signal. 21 2009 1287 1297
    • (2009) Cell. Signal. , vol.21 , pp. 1287-1297
    • Babuke, T.1    Ruonala, M.2    Meister, M.3    Amaddii, M.4    Genzler, C.5    Esposito, A.6    Tikkanen, R.7
  • 47
    • 84879430920 scopus 로고    scopus 로고
    • Sites of reactive oxygen species generation by mitochondria oxidizing different substrates
    • C.L. Quinlan, I.V. Perevoshchikova, M. Hey-Mogensen, A.L. Orr, and M.D. Brand Sites of reactive oxygen species generation by mitochondria oxidizing different substrates Redox Biol. 1 2013 304 312
    • (2013) Redox Biol. , vol.1 , pp. 304-312
    • Quinlan, C.L.1    Perevoshchikova, I.V.2    Hey-Mogensen, M.3    Orr, A.L.4    Brand, M.D.5
  • 48
    • 4043090717 scopus 로고    scopus 로고
    • Superoxide production by NADH: Ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane
    • A.J. Lambert, and M.D. Brand Superoxide production by NADH: ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane Biochem. J. 382 2004 511 517
    • (2004) Biochem. J. , vol.382 , pp. 511-517
    • Lambert, A.J.1    Brand, M.D.2


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