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Volumn 62, Issue 13, 2005, Pages 1478-1488

Identification of tyrosine-phosphorylated proteins of the mitochondrial oxidative phosphorylation machinery

Author keywords

Mitochondria; Oxidant; Oxidative phosphorylation; PTP 1B; Src kinase; Tyrosine phosphorylation

Indexed keywords

4 AMINO 7 TERT BUTYL 5 (4 CHLOROPHENYL)PYRAZOLO[3,4 D]PYRIMIDINE; ADENOSINE TRIPHOSPHATE; FLUSHED OVIDUCAL FLUID PROTEIN 1; HYDROGEN PEROXIDE; METALLOPROTEINASE INHIBITOR; MITOCHONDRIAL PROTEIN; PROTEIN; PROTEIN SUBUNIT; PROTEIN TYROSINE PHOSPHATASE 1B; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REACTIVE OXYGEN METABOLITE; TYROSINE; UNCLASSIFIED DRUG;

EID: 21544448596     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-005-5005-7     Document Type: Article
Times cited : (64)

References (44)
  • 1
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B., Sies H. and Boveris A. (1979) Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59: 527-605
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 2
    • 0033369476 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical generation and leak: Sites of production in states 4 and 3, organ specificity, and relation to aging and longevity
    • Barja G. (1999) Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity, and relation to aging and longevity. J. Bioenerg. Biomemb. 31: 347-366
    • (1999) J. Bioenerg. Biomemb. , vol.31 , pp. 347-366
    • Barja, G.1
  • 3
    • 0034705703 scopus 로고    scopus 로고
    • Protein phosphorylation/dephosphorylation in the inner membrane of potato tuber mitochondria
    • Struglics A., Fredlund K. M., Konstantinov Y. M., Allen J. F. and Moller I. M. (2000) Protein phosphorylation/dephosphorylation in the inner membrane of potato tuber mitochondria. FEBS Lett. 475: 213-217
    • (2000) FEBS Lett. , vol.475 , pp. 213-217
    • Struglics, A.1    Fredlund, K.M.2    Konstantinov, Y.M.3    Allen, J.F.4    Moller, I.M.5
  • 4
    • 0032562028 scopus 로고    scopus 로고
    • Two subunits of the FoF1-ATPase are phosphorylated in the inner mitochondrial membrane
    • Struglics A., Fredlund K. M., Allen J. F. and Moller I. M. (1998) Two subunits of the FoF1-ATPase are phosphorylated in the inner mitochondrial membrane. Biochem. Biophys. Res. Commun. 243: 664-668
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 664-668
    • Struglics, A.1    Fredlund, K.M.2    Allen, J.F.3    Moller, I.M.4
  • 5
    • 0034993923 scopus 로고    scopus 로고
    • Protein phosphorylation in mitochondria from human placenta
    • Corso M. and Thomson M. (2001) Protein phosphorylation in mitochondria from human placenta. Placenta 22: 432-439
    • (2001) Placenta , vol.22 , pp. 432-439
    • Corso, M.1    Thomson, M.2
  • 7
    • 2442714587 scopus 로고    scopus 로고
    • Control of mitochondrial membrane potential and ROS formation by reversible phosphorylation of cytochrome c oxidase
    • Lee I., Bender E. and Kadenbach B. (2002) Control of mitochondrial membrane potential and ROS formation by reversible phosphorylation of cytochrome c oxidase. Mol. Cell. Biochem. 234/235: 63-70
    • (2002) Mol. Cell. Biochem. , vol.234-235 , pp. 63-70
    • Lee, I.1    Bender, E.2    Kadenbach, B.3
  • 8
    • 0037431026 scopus 로고    scopus 로고
    • Identification of 14 new phosphoproteins involved in important plant mitochondrial processes
    • Bykova N. V., Egsgaard H. and Moller I. M. (2003) Identification of 14 new phosphoproteins involved in important plant mitochondrial processes. FEBS Lett. 540: 141-146
    • (2003) FEBS Lett. , vol.540 , pp. 141-146
    • Bykova, N.V.1    Egsgaard, H.2    Moller, I.M.3
  • 9
    • 0038034950 scopus 로고    scopus 로고
    • Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye
    • Schulenberg B., Aggeler R., Beechem J. M., Capaldi R. A. and Patton W. F. (2003) Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye. J. Biol. Chem. 278: 27251-27255
    • (2003) J. Biol. Chem. , vol.278 , pp. 27251-27255
    • Schulenberg, B.1    Aggeler, R.2    Beechem, J.M.3    Capaldi, R.A.4    Patton, W.F.5
  • 10
    • 2942726285 scopus 로고    scopus 로고
    • The phosphorylation of subunits of complex I from bovine heart mitochondria
    • Chen R., Fearnley I. M., Peak-Chew S. Y. and Walker J. E. (2004) The phosphorylation of subunits of complex I from bovine heart mitochondria. J. Biol. Chem. 279: 26036-26045
    • (2004) J. Biol. Chem. , vol.279 , pp. 26036-26045
    • Chen, R.1    Fearnley, I.M.2    Peak-Chew, S.Y.3    Walker, J.E.4
  • 11
    • 0023829933 scopus 로고
    • Identification and characterization of tyrosine kinase activity associated with mitochondrial outer membrane in sarcoma 180 cells
    • Piedimonte G., Chamaret S., Dauget C., Borghetti A. F. and Montagnier L. (1988) Identification and characterization of tyrosine kinase activity associated with mitochondrial outer membrane in sarcoma 180 cells. J. Cell. Biochem. 39: 91-102
    • (1988) J. Cell. Biochem. , vol.39 , pp. 91-102
    • Piedimonte, G.1    Chamaret, S.2    Dauget, C.3    Borghetti, A.F.4    Montagnier, L.5
  • 12
    • 0023841587 scopus 로고
    • Enhancement of mitochondrial tyrosine kinase activity following viral transformation
    • Piedimonte G., Silvotti L., Borghetti A. F. and Montagnier L. (1988) Enhancement of mitochondrial tyrosine kinase activity following viral transformation. Cancer Lett. 39: 1-8
    • (1988) Cancer Lett. , vol.39 , pp. 1-8
    • Piedimonte, G.1    Silvotti, L.2    Borghetti, A.F.3    Montagnier, L.4
  • 13
    • 0037012576 scopus 로고    scopus 로고
    • Characterization and location of Src-dependent tyrosine phosphorylation in rat brain mitochondria. Biochim
    • Salvi M., Brunati A. M., Bordin L., La Rocca N., Clari G. and Toninello A. (2002) Characterization and location of Src-dependent tyrosine phosphorylation in rat brain mitochondria. Biochim. Biophys. Acta 1589: 181-195
    • (2002) Biophys. Acta , vol.1589 , pp. 181-195
    • Salvi, M.1    Brunati, A.M.2    Bordin, L.3    La Rocca, N.4    Clari, G.5    Toninello, A.6
  • 14
    • 0037416134 scopus 로고    scopus 로고
    • Regulation of cytochrome c oxidase activity by c-Src in osteoclasts
    • Miyazaki T., Neff L., Tanaka S., Horne W. C. and Baron R. (2003) Regulation of cytochrome c oxidase activity by c-Src in osteoclasts. J. Cell. Biol. 160: 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
  • 15
    • 0036210579 scopus 로고    scopus 로고
    • Signal transduction to mitochondrial ATP synthase: Evidence that PDGF-dependent phosphorylation of the γ-subunit occurs in several cell lines, involves tyrosine, and is modulated by lysophosphatidic acid
    • Ko Y. H., Pan W., Inoue C. and Pedersen P. L. (2002) Signal transduction to mitochondrial ATP synthase: evidence that PDGF-dependent phosphorylation of the γ-subunit occurs in several cell lines, involves tyrosine, and is modulated by lysophosphatidic acid. Mitochondrion 1: 339-348
    • (2002) Mitochondrion , vol.1 , pp. 339-348
    • Ko, Y.H.1    Pan, W.2    Inoue, C.3    Pedersen, P.L.4
  • 16
    • 0037070143 scopus 로고    scopus 로고
    • Serine (threonine) phosphatase(s) acting on cAMP-dependent phosphoproteins in mammalian mitochondria
    • Signorile A., Sardanelli A. M., Nuzzi R. and Papa S. (2002) Serine (threonine) phosphatase(s) acting on cAMP-dependent phosphoproteins in mammalian mitochondria. FEBS Lett. 512: 91-94
    • (2002) FEBS Lett. , vol.512 , pp. 91-94
    • Signorile, A.1    Sardanelli, A.M.2    Nuzzi, R.3    Papa, S.4
  • 17
    • 6044236768 scopus 로고    scopus 로고
    • Tyrosine phosphatase activity in mitochondria: Presence of Shp-2 phosphatase in mitochondria
    • Salvi M., Stingaro A., Brunati A. M, Agostinelli E and Arancia G. (2004) Tyrosine phosphatase activity in mitochondria: presence of Shp-2 phosphatase in mitochondria. Cell Mol Life Sci. 61: 2393-2404
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 2393-2404
    • Salvi, M.1    Stingaro, A.2    Brunati, A.M.3    Agostinelli, E.4    Arancia, G.5
  • 18
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • Finkel T. (1998) Oxygen radicals and signaling. Curr. Opin. Cell. Biol. 10: 248-253
    • (1998) Curr. Opin. Cell. Biol. , vol.10 , pp. 248-253
    • Finkel, T.1
  • 19
    • 0034255470 scopus 로고    scopus 로고
    • Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH
    • Kim J. R., Yoon H. W., Kwon K. S., Lee S. R. and Rhee S. G. (2000) Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH. Anal. Biochem. 283: 214-221
    • (2000) Anal. Biochem. , vol.283 , pp. 214-221
    • Kim, J.R.1    Yoon, H.W.2    Kwon, K.S.3    Lee, S.R.4    Rhee, S.G.5
  • 20
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu J. M. and Tanner K. G. (1998) Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37: 5633-5642
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 21
    • 0014962720 scopus 로고
    • The metabolism of rat brain mitochondria. Preparation and characterization
    • Clark J. B. and Nicklas W. J. (1970) The metabolism of rat brain mitochondria. Preparation and characterization. J. Biol. Chem. 245: 4724-4731
    • (1970) J. Biol. Chem. , vol.245 , pp. 4724-4731
    • Clark, J.B.1    Nicklas, W.J.2
  • 23
    • 21544436710 scopus 로고
    • Relationships between age-dependent changes in the effect of almitrine on H(+)-ATPase/ATPsynthase and the pattern of membrane fatty acid composition
    • Jumelle-Laclau M., Rigoulet M., Averet N., Leverve X., Dubourg L., Carbonneau A. et al. (1993) Relationships between age-dependent changes in the effect of almitrine on H(+)-ATPase/ATPsynthase and the pattern of membrane fatty acid composition. Biochim. Biophys. Acta 114: 190-194.
    • (1993) Biochim. Biophys. Acta , vol.114 , pp. 190-194
    • Jumelle-Laclau, M.1    Rigoulet, M.2    Averet, N.3    Leverve, X.4    Dubourg, L.5    Carbonneau, A.6
  • 24
    • 1842562333 scopus 로고    scopus 로고
    • Mitochondrial extracellular signal-regulated kinases 1/2 (ERK1/2) are modulated during brain development
    • Alonso M., Melani M., Converse D., Jaitovich A., Paz C., Carreras M. C. et al. (2004) Mitochondrial extracellular signal-regulated kinases 1/2 (ERK1/2) are modulated during brain development. J. Neurochem. 89: 248-256.
    • (2004) J. Neurochem. , vol.89 , pp. 248-256
    • Alonso, M.1    Melani, M.2    Converse, D.3    Jaitovich, A.4    Paz, C.5    Carreras, M.C.6
  • 25
    • 2042432480 scopus 로고
    • Cytochrome oxidase from beef heart mitochondria
    • Estabrook R. and Pullman M. (eds), Academic Press, New York
    • Wharton D. and Tzagoloff A. (1967) Cytochrome oxidase from beef heart mitochondria. In: Methods in Enzymology, pp. 245-250, Estabrook R. and Pullman M. (eds), Academic Press, New York
    • (1967) Methods in Enzymology , pp. 245-250
    • Wharton, D.1    Tzagoloff, A.2
  • 26
    • 0036231792 scopus 로고    scopus 로고
    • Cytochrome c oxidase and mitochondrial F1Fo-ATPase (ATP synthase) activities in platelets and brain from patients with Alzheimer's disease
    • Bosetti F., Brizzi F., Barogi S., Mancusso M., Siciliano G., Tendi E. A. et al. (2002) Cytochrome c oxidase and mitochondrial F1Fo-ATPase (ATP synthase) activities in platelets and brain from patients with Alzheimer's disease. Neurobiol. Aging 23: 371-376
    • (2002) Neurobiol. Aging , vol.23 , pp. 371-376
    • Bosetti, F.1    Brizzi, F.2    Barogi, S.3    Mancusso, M.4    Siciliano, G.5    Tendi, E.A.6
  • 27
    • 0021160336 scopus 로고
    • A quantitative fluorimetric assay for the determination of oxidant production by polymorphonuclear leukocytes: Its use in the simultaneous fluorimetric assay of cellular activation processes
    • Hyslop P. A. and Sklar A. (1984) A quantitative fluorimetric assay for the determination of oxidant production by polymorphonuclear leukocytes: its use in the simultaneous fluorimetric assay of cellular activation processes. Anal. Biochem. 141: 280-286
    • (1984) Anal. Biochem. , vol.141 , pp. 280-286
    • Hyslop, P.A.1    Sklar, A.2
  • 29
    • 0035222647 scopus 로고    scopus 로고
    • Blue-native gels to isolate protein complexes from mitochondria
    • Schagger H. (2001) Blue-native gels to isolate protein complexes from mitochondria. Methods Cell Biol. 65: 231-244
    • (2001) Methods Cell Biol. , vol.65 , pp. 231-244
    • Schagger, H.1
  • 30
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger H. and Jagow G. von (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199: 223-231
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    Von Jagow, G.2
  • 31
    • 0030853263 scopus 로고    scopus 로고
    • Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels
    • Zerbetto E., Vergani L. and Dabbeni-Sala F. (1997) Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels. Electrophoresis 18: 2059-2064
    • (1997) Electrophoresis , vol.18 , pp. 2059-2064
    • Zerbetto, E.1    Vergani, L.2    Dabbeni-Sala, F.3
  • 32
    • 1542290022 scopus 로고    scopus 로고
    • Cytochrome c oxidase subassemblies in fibroblast cultures from patients carrying mutations in COX10, SCO1, or SURF1
    • Williams S. L., Valnot I., Rustin P. and Taanman J. W. (2003) Cytochrome c oxidase subassemblies in fibroblast cultures from patients carrying mutations in COX10, SCO1, or SURF1. J. Biol. Chem. 279: 7462-7469
    • (2003) J. Biol. Chem. , vol.279 , pp. 7462-7469
    • Williams, S.L.1    Valnot, I.2    Rustin, P.3    Taanman, J.W.4
  • 33
    • 0038199726 scopus 로고    scopus 로고
    • PTP1B: From the sidelines to the front lines!
    • Tonks N. K. (2003) PTP1B: from the sidelines to the front lines! FEBS Lett. 546: 140-148
    • (2003) FEBS Lett. , vol.546 , pp. 140-148
    • Tonks, N.K.1
  • 34
    • 0034731372 scopus 로고    scopus 로고
    • Identification of protein tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines
    • Bjorge J. D., Pang A. and Fujita D. J. (2000) Identification of protein tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines. J. Biol. Chem. 275: 41439-41446
    • (2000) J. Biol. Chem. , vol.275 , pp. 41439-41446
    • Bjorge, J.D.1    Pang, A.2    Fujita, D.J.3
  • 35
    • 0022446434 scopus 로고
    • Phosphorylation and inactivation of protein phosphatase 1 by pp60v-src
    • Johansen J. W. and Ingebritsen T. S. (1986) Phosphorylation and inactivation of protein phosphatase 1 by pp60v-src. Proc. Natl. Acad. Sci. USA 83: 207-211
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 207-211
    • Johansen, J.W.1    Ingebritsen, T.S.2
  • 36
    • 0026584285 scopus 로고
    • The non transmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence
    • Frangioni J. V., Beahm P. H., Shifrin V., Jost C. A. and Neel B. G. (1992) The non transmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence. Cell 68: 545-560
    • (1992) Cell , vol.68 , pp. 545-560
    • Frangioni, J.V.1    Beahm, P.H.2    Shifrin, V.3    Jost, C.A.4    Neel, B.G.5
  • 37
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: An update
    • Bain J., McLauchlan H., Elliott M. and Cohen P. (2003) The specificities of protein kinase inhibitors: an update. Biochem. J. 371: 199-204
    • (2003) Biochem. J. , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 38
    • 0036183196 scopus 로고    scopus 로고
    • Evidence of undiscovered cell regulatory mechanisms: Phosphoproteins and protein kinases in mitochondria
    • Thomson M. (2002) Evidence of undiscovered cell regulatory mechanisms: phosphoproteins and protein kinases in mitochondria. Cell. Mol. Life Sci. 59: 213-219
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 213-219
    • Thomson, M.1
  • 41
    • 0033584845 scopus 로고    scopus 로고
    • Threshold effect and tissue specificity: Implication for mitochondrial cytopathies
    • Rossignol R., Malgat M., Mazat J.-P. and Letellier T. (1999) Threshold effect and tissue specificity: implication for mitochondrial cytopathies. J. Biol. Chem. 274: 33426-33432
    • (1999) J. Biol. Chem. , vol.274 , pp. 33426-33432
    • Rossignol, R.1    Malgat, M.2    Mazat, J.-P.3    Letellier, T.4
  • 42
    • 0037189477 scopus 로고    scopus 로고
    • Proteomic analysis of protein phosphorylations in heat shock response and thermotolerance
    • Kim H. J., Song E. J. and Lee K. J. (2002) Proteomic analysis of protein phosphorylations in heat shock response and thermotolerance. J. Biol. Chem. 277: 23193-23207
    • (2002) J. Biol. Chem. , vol.277 , pp. 23193-23207
    • Kim, H.J.1    Song, E.J.2    Lee, K.J.3
  • 43
    • 0034120638 scopus 로고    scopus 로고
    • Matrix assisted laser desorption/ionization-time of flight-mass spectrometry analysis of proteins detected by anti-phosphotyrosine antibody on two-dimensional-gels of fibroblast cell lysates after tumor necrosis factor-alpha stimulation
    • Yanagida M., Miura Y., Yagasaki K., Taoka M., Isobe T. and Takahashi N. (2000) Matrix assisted laser desorption/ionization-time of flight-mass spectrometry analysis of proteins detected by anti-phosphotyrosine antibody on two-dimensional-gels of fibroblast cell lysates after tumor necrosis factor-alpha stimulation. Electrophoresis 21: 190-198
    • (2000) Electrophoresis , vol.21 , pp. 190-198
    • Yanagida, M.1    Miura, Y.2    Yagasaki, K.3    Taoka, M.4    Isobe, T.5    Takahashi, N.6


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