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Volumn 410, Issue 1, 2008, Pages 195-204

Activation and stabilization of human tryptophan hydroxylase 2 by phosphorylation and 14-3-3 binding

Author keywords

14 3 3 protein; Human embryonic kidney (HEK) 293 cell; Phosphorylation; Protein kinase A; Serotonin; Tryptophan hydroxylase 2 (TPH2) regulation

Indexed keywords

BINDING SITES; ESCHERICHIA COLI; PHOSPHORYLATION; STOICHIOMETRY; TISSUE;

EID: 39749177631     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071033     Document Type: Article
Times cited : (61)

References (48)
  • 1
    • 0034929271 scopus 로고    scopus 로고
    • A structural approach into human tryptophan hydroxylase and its implications for the regulation of serotonin biosynthesis
    • Martinez, A., Knappskog, P. M. and Haavik, J. (2001) A structural approach into human tryptophan hydroxylase and its implications for the regulation of serotonin biosynthesis. Curr. Med. Chem. 8, 1077-1091
    • (2001) Curr. Med. Chem , vol.8 , pp. 1077-1091
    • Martinez, A.1    Knappskog, P.M.2    Haavik, J.3
  • 3
    • 33847222673 scopus 로고    scopus 로고
    • Selectivity and affinity determinants for ligand binding to the aromatic amino acid hydroxylases
    • Teigen, K., McKinney, J., Haavik, J. and Martínez, A. (2007) Selectivity and affinity determinants for ligand binding to the aromatic amino acid hydroxylases. Curr. Med. Chem. 14, 455-467
    • (2007) Curr. Med. Chem , vol.14 , pp. 455-467
    • Teigen, K.1    McKinney, J.2    Haavik, J.3    Martínez, A.4
  • 5
    • 0141922899 scopus 로고    scopus 로고
    • A unique central tryptophan hydroxylase isoform
    • Walther, D. J. and Bader, M. (2003) A unique central tryptophan hydroxylase isoform. Biochem. Pharmacol. 66, 1673-1680
    • (2003) Biochem. Pharmacol , vol.66 , pp. 1673-1680
    • Walther, D.J.1    Bader, M.2
  • 6
    • 13244292476 scopus 로고    scopus 로고
    • Different properties of the central and peripheral forms of human tryptophan hydroxylase
    • McKinney, J., Knappskog, P. M. and Haavik, J. (2005) Different properties of the central and peripheral forms of human tryptophan hydroxylase. J. Neurochem. 92, 311-320
    • (2005) J. Neurochem , vol.92 , pp. 311-320
    • McKinney, J.1    Knappskog, P.M.2    Haavik, J.3
  • 7
    • 0030050954 scopus 로고    scopus 로고
    • Phosphorylation and activation of tryptophan hydroxylase by exogenous protein kinase A
    • Johansen, P. A., Jennings, I., Cotton, R. G. and Kuhn, D. M. (1996) Phosphorylation and activation of tryptophan hydroxylase by exogenous protein kinase A. J. Neurochem. 66, 817-823
    • (1996) J. Neurochem , vol.66 , pp. 817-823
    • Johansen, P.A.1    Jennings, I.2    Cotton, R.G.3    Kuhn, D.M.4
  • 8
    • 0023602004 scopus 로고
    • Regulation of tryptophan hydroxylase activity by a cyclic AMP-dependent mechanism in rat striatum
    • Garber, S. L. and Makman, M. H. (1987) Regulation of tryptophan hydroxylase activity by a cyclic AMP-dependent mechanism in rat striatum. Brain. Res. 427, 1-10
    • (1987) Brain. Res , vol.427 , pp. 1-10
    • Garber, S.L.1    Makman, M.H.2
  • 9
    • 0017887515 scopus 로고
    • Activation of tryptophan hydroxylase by adenosine triphosphate, magnesium, and calcium
    • Hamon, M., Bourgoin, S., Hery, F., and Simonnet, G. (1978) Activation of tryptophan hydroxylase by adenosine triphosphate, magnesium, and calcium. Mol. Pharmacol. 14, 99-110
    • (1978) Mol. Pharmacol , vol.14 , pp. 99-110
    • Hamon, M.1    Bourgoin, S.2    Hery, F.3    Simonnet, G.4
  • 10
    • 0018688641 scopus 로고
    • Activation of tryptophan 5-monooxygenase by calcium-dependent regulator protein
    • Yamauchi, T. and Fujisawa, H. (1979) Activation of tryptophan 5-monooxygenase by calcium-dependent regulator protein. Biochem. Biophys. Res. Commun. 90, 28-35
    • (1979) Biochem. Biophys. Res. Commun , vol.90 , pp. 28-35
    • Yamauchi, T.1    Fujisawa, H.2
  • 12
    • 0028892956 scopus 로고
    • Identification of the site of interaction of the 14-3-3 protein with phosphorylated tryptophan hydroxylase
    • Ichimura, T., Uchiyama, J., Kunihiro, O., Ito, M., Horigome, T., Omata, S., Shinkai, F., Kaji, H. and Isobe, T. (1995) Identification of the site of interaction of the 14-3-3 protein with phosphorylated tryptophan hydroxylase. J. Biol. Chem. 270, 28515-28518
    • (1995) J. Biol. Chem , vol.270 , pp. 28515-28518
    • Ichimura, T.1    Uchiyama, J.2    Kunihiro, O.3    Ito, M.4    Horigome, T.5    Omata, S.6    Shinkai, F.7    Kaji, H.8    Isobe, T.9
  • 14
    • 0030924507 scopus 로고    scopus 로고
    • Amino-terminal analysis of tryptophan hydroxylase: Protein kinase phosphorylation occurs at serine-58
    • Kumer, S. C., Mockus, S. M., Rucker, P. J. and Vrana, K. E. (1997) Amino-terminal analysis of tryptophan hydroxylase: protein kinase phosphorylation occurs at serine-58. J. Neurochem. 69, 1738-1745
    • (1997) J. Neurochem , vol.69 , pp. 1738-1745
    • Kumer, S.C.1    Mockus, S.M.2    Rucker, P.J.3    Vrana, K.E.4
  • 15
    • 0030898129 scopus 로고    scopus 로고
    • Phosphorylation and activation of brain tryptophan hydroxylase: Identification of serine-58 as a substrate site for protein kinase A
    • Kuhn, D. M., Arthur, Jr, R. and States, J. C. (1997) Phosphorylation and activation of brain tryptophan hydroxylase: identification of serine-58 as a substrate site for protein kinase A. J. Neurochem. 68, 2220-2223
    • (1997) J. Neurochem , vol.68 , pp. 2220-2223
    • Kuhn, D.M.1    Arthur Jr, R.2    States, J.C.3
  • 16
    • 0034730416 scopus 로고    scopus 로고
    • Identification of substrate orienting and phosphorylation sites within tryptophan hydroxylase using homology-based molecular modeling
    • Jiang, G. C., Yohrling, 4th, G. J., Schmitt, J. D. and Vrana, K. E. (2000) Identification of substrate orienting and phosphorylation sites within tryptophan hydroxylase using homology-based molecular modeling. J. Mol. Biol. 302, 1005-1017
    • (2000) J. Mol. Biol , vol.302 , pp. 1005-1017
    • Jiang, G.C.1    Yohrling 4th, G.J.2    Schmitt, J.D.3    Vrana, K.E.4
  • 17
    • 0036399655 scopus 로고    scopus 로고
    • Proteasome-driven turnover of tryptophan hydroxylase is triggered by phosphorylation in RBL2H3 cells, a serotonin producing mast cell line
    • Iida, Y., Sawabe, K., Kojima, M., Oguro, K., Nakanishi, N. and Hasegawa, H. (2002) Proteasome-driven turnover of tryptophan hydroxylase is triggered by phosphorylation in RBL2H3 cells, a serotonin producing mast cell line. Eur. J. Biochem. 269, 4780-4788
    • (2002) Eur. J. Biochem , vol.269 , pp. 4780-4788
    • Iida, Y.1    Sawabe, K.2    Kojima, M.3    Oguro, K.4    Nakanishi, N.5    Hasegawa, H.6
  • 19
    • 33646926129 scopus 로고    scopus 로고
    • 14-3-3 proteins: A historic overview
    • Aitken, A. (2006) 14-3-3 proteins: a historic overview. Semin. Cancer Biol. 16, 162-172
    • (2006) Semin. Cancer Biol , vol.16 , pp. 162-172
    • Aitken, A.1
  • 20
    • 0005312677 scopus 로고
    • Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, a protein kinase-dependent activator of tyrosine and tryptophan hydroxylases
    • Ichimura, T., Isobe, T., Okuyama, T., Takahashi, N., Araki, K., Kuwano, R. and Takahashi, Y. (1988) Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, a protein kinase-dependent activator of tyrosine and tryptophan hydroxylases. Proc. Natl. Acad. Sci. U.S.A. 85, 7084-7088
    • (1988) Proc. Natl. Acad. Sci. U.S.A , vol.85 , pp. 7084-7088
    • Ichimura, T.1    Isobe, T.2    Okuyama, T.3    Takahashi, N.4    Araki, K.5    Kuwano, R.6    Takahashi, Y.7
  • 21
    • 0023652643 scopus 로고
    • Brain 14-3-3 protein is an activator protein that activates tryptophan 5-monooxygenase and tyrosine 3-monooxygenase in the presence of Ca2+,calmodulin-dependent protein kinase II
    • Ichimura, T., Isobe, T., Okuyama, T., Yamauchi, T. and Fujisawa, H. (1987) Brain 14-3-3 protein is an activator protein that activates tryptophan 5-monooxygenase and tyrosine 3-monooxygenase in the presence of Ca2+,calmodulin-dependent protein kinase II. FEBS Lett. 219, 79-82
    • (1987) FEBS Lett , vol.219 , pp. 79-82
    • Ichimura, T.1    Isobe, T.2    Okuyama, T.3    Yamauchi, T.4    Fujisawa, H.5
  • 22
    • 33847714370 scopus 로고    scopus 로고
    • Characterization of wild-type and mutant forms of human tryptophan hydroxylase 2
    • Winge, I., McKinney, J. A., Knappskog, P. M. and Haavik, J. (2007) Characterization of wild-type and mutant forms of human tryptophan hydroxylase 2. J. Neurochem. 100, 1648-1657
    • (2007) J. Neurochem , vol.100 , pp. 1648-1657
    • Winge, I.1    McKinney, J.A.2    Knappskog, P.M.3    Haavik, J.4
  • 23
    • 0035019161 scopus 로고    scopus 로고
    • Interaction of phosphorylated tyrosine hydroxylase with 14-3-3 proteins: Evidence for a phosphoserine 40-dependent association
    • Kleppe, R., Toska, K. and Haavik, J. (2001) Interaction of phosphorylated tyrosine hydroxylase with 14-3-3 proteins: evidence for a phosphoserine 40-dependent association. J. Neurochem. 77, 1097-1107
    • (2001) J. Neurochem , vol.77 , pp. 1097-1107
    • Kleppe, R.1    Toska, K.2    Haavik, J.3
  • 25
    • 0019179348 scopus 로고
    • Fluorometric detection of tryptophan, 5-hydroxytryptophan, and 5-hydroxytryptamine (serotonin) in high-performance liquid chromatography
    • Flatmark, T., Jacobsen, S. W. and Haavik, J. (1980) Fluorometric detection of tryptophan, 5-hydroxytryptophan, and 5-hydroxytryptamine (serotonin) in high-performance liquid chromatography. Anal. Biochem. 107, 71-74
    • (1980) Anal. Biochem , vol.107 , pp. 71-74
    • Flatmark, T.1    Jacobsen, S.W.2    Haavik, J.3
  • 26
    • 0035951089 scopus 로고    scopus 로고
    • Conformation of the substrate and pterin cofactor bound to human tryptophan hydroxylase. Important role of Phe313 in substrate specificity
    • McKinney, J., Teigen, K., Froystein, N. A., Salaun, C., Knappskog, P. M., Haavik, J. and Martinez, A. (2001) Conformation of the substrate and pterin cofactor bound to human tryptophan hydroxylase. Important role of Phe313 in substrate specificity. Biochemistry 40, 15591-15601
    • (2001) Biochemistry , vol.40 , pp. 15591-15601
    • McKinney, J.1    Teigen, K.2    Froystein, N.A.3    Salaun, C.4    Knappskog, P.M.5    Haavik, J.6    Martinez, A.7
  • 27
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen, M. R., Thingholm, T. E., Jensen, O. N., Roepstorff, P. and Jorgensen, T. J. (2005) Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell. Proteomics 4, 873-886
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jorgensen, T.J.5
  • 28
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoL C-ESI-MS/MS and titanium oxide precolumns
    • Pinkse, M. W., Uitto, P. M., Hilhorst, M. J., Ooms, B. and Heck, A. J. (2004) Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoL C-ESI-MS/MS and titanium oxide precolumns. Anal. Chem. 76, 3935-3943
    • (2004) Anal. Chem , vol.76 , pp. 3935-3943
    • Pinkse, M.W.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.5
  • 29
    • 0030008190 scopus 로고    scopus 로고
    • PKU mutation G46S is associated with increased aggregation and degradation of the phenylalanine hydroxylase enzyme
    • Eiken, H. G., Knappskog, P. M., Apold, J. and Flatmark, T. (1996) PKU mutation G46S is associated with increased aggregation and degradation of the phenylalanine hydroxylase enzyme. Hum. Mutat. 7, 228-238
    • (1996) Hum. Mutat , vol.7 , pp. 228-238
    • Eiken, H.G.1    Knappskog, P.M.2    Apold, J.3    Flatmark, T.4
  • 30
    • 0029796673 scopus 로고    scopus 로고
    • PKU mutation (D143G) associated with an apparent high residual enzyme activity: Expression of a kinetic variant form of phenylalanine hydroxylase in three different systems
    • Knappskog, P. M., Eiken, H. G., Martinez, A., Bruland, O., Apold, J. and Flatmark, T. (1996) PKU mutation (D143G) associated with an apparent high residual enzyme activity: expression of a kinetic variant form of phenylalanine hydroxylase in three different systems. Hum. Mutat. 8, 236-246
    • (1996) Hum. Mutat , vol.8 , pp. 236-246
    • Knappskog, P.M.1    Eiken, H.G.2    Martinez, A.3    Bruland, O.4    Apold, J.5    Flatmark, T.6
  • 31
    • 35449003540 scopus 로고    scopus 로고
    • Phosphorylation and activation of tryptophan hydroxylase 2: Identification of serine-19 as the substrate site for calcium, calmodulin-dependent protein kinase II
    • Kuhn, D. M., Sakowski, S. A., Geddes, T. J., Wilkerson, C. and Haycock, J. W. (2007) Phosphorylation and activation of tryptophan hydroxylase 2: identification of serine-19 as the substrate site for calcium, calmodulin-dependent protein kinase II. J. Neurochem. 103, 1567-1573
    • (2007) J. Neurochem , vol.103 , pp. 1567-1573
    • Kuhn, D.M.1    Sakowski, S.A.2    Geddes, T.J.3    Wilkerson, C.4    Haycock, J.W.5
  • 33
    • 0027508290 scopus 로고
    • Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2
    • Sutherland, C., Alterio, J., Campbell, D. G., Le Bourdelles, B., Mallet, J., Haavik, J. and Cohen, P. (1993) Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2. Eur. J. Biochem. 217, 715-722
    • (1993) Eur. J. Biochem , vol.217 , pp. 715-722
    • Sutherland, C.1    Alterio, J.2    Campbell, D.G.3    Le Bourdelles, B.4    Mallet, J.5    Haavik, J.6    Cohen, P.7
  • 35
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • Blom, N., Sicheritz-Ponten, T., Gupta, R., Gammeltoft, S. and Brunak, S. (2004) Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4, 1633-1649
    • (2004) Proteomics , vol.4 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Ponten, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, S.5
  • 36
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases
    • Kennelly, P. J. and Krebs, E. G. (1991) Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J. Biol. Chem. 266, 15555-15558
    • (1991) J. Biol. Chem , vol.266 , pp. 15555-15558
    • Kennelly, P.J.1    Krebs, E.G.2
  • 38
    • 0028037550 scopus 로고
    • Cloning and expression of rabbit and human brain tryptophan hydroxylase cDNA in Escherichia coli
    • Tipper, J. P., Citron, B. A., Ribeiro, P. and Kaufman, S. (1994) Cloning and expression of rabbit and human brain tryptophan hydroxylase cDNA in Escherichia coli. Arch. Biochem. Biophys. 315, 445-453
    • (1994) Arch. Biochem. Biophys , vol.315 , pp. 445-453
    • Tipper, J.P.1    Citron, B.A.2    Ribeiro, P.3    Kaufman, S.4
  • 39
    • 11444260122 scopus 로고    scopus 로고
    • Mutation of regulatory serines of rat tyrosine hydroxylase to glutamate: Effects on enzyme stability and activity
    • Royo, M., Fitzpatrick, P. F. and Daubner, S. C. (2005) Mutation of regulatory serines of rat tyrosine hydroxylase to glutamate: effects on enzyme stability and activity. Arch. Biochem. Biophys. 434, 266-274
    • (2005) Arch. Biochem. Biophys , vol.434 , pp. 266-274
    • Royo, M.1    Fitzpatrick, P.F.2    Daubner, S.C.3
  • 40
    • 33745840805 scopus 로고    scopus 로고
    • Differential regulation of the human tyrosine hydroxylase isoforms via hierarchical phosphorylation
    • Lehmann, I. T., Bobrovskaya, L., Gordon, S. L., Dunkley, P. R. and Dickson, P. W. (2006) Differential regulation of the human tyrosine hydroxylase isoforms via hierarchical phosphorylation. J. Biol. Chem. 281, 17644-17651
    • (2006) J. Biol. Chem , vol.281 , pp. 17644-17651
    • Lehmann, I.T.1    Bobrovskaya, L.2    Gordon, S.L.3    Dunkley, P.R.4    Dickson, P.W.5
  • 41
    • 33750725388 scopus 로고    scopus 로고
    • Analysis of tryptophan hydroxylase I and II mRNA expression in the human brain: A post-mortem study
    • Zill, P., Buttner, A., Eisenmenger, W., Moller, H. J., Ackenheil, M. and Bondy, B. (2007) Analysis of tryptophan hydroxylase I and II mRNA expression in the human brain: A post-mortem study. J. Psychiatr. Res. 41, 168-173
    • (2007) J. Psychiatr. Res , vol.41 , pp. 168-173
    • Zill, P.1    Buttner, A.2    Eisenmenger, W.3    Moller, H.J.4    Ackenheil, M.5    Bondy, B.6
  • 43
    • 0034661857 scopus 로고    scopus 로고
    • Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155
    • Lizcano, J. M., Morrice, N. and Cohen, P. (2000) Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155. Biochem. J. 349, 547-557
    • (2000) Biochem. J , vol.349 , pp. 547-557
    • Lizcano, J.M.1    Morrice, N.2    Cohen, P.3
  • 44
    • 29244476034 scopus 로고    scopus 로고
    • The regulatory phosphorylated serine in full-length nitrate reductase is necessary for optimal binding to a 14-3-3 protein
    • Provan, F., Haavik, J. and Lillo, C. (2006) The regulatory phosphorylated serine in full-length nitrate reductase is necessary for optimal binding to a 14-3-3 protein. Plant Sci. 170, 394-398
    • (2006) Plant Sci , vol.170 , pp. 394-398
    • Provan, F.1    Haavik, J.2    Lillo, C.3
  • 45
    • 0032055050 scopus 로고    scopus 로고
    • Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins
    • Ku, N. O., Liao, J. and Omary, M. B. (1998) Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins. EMBO J. 17, 1892-1906
    • (1998) EMBO J , vol.17 , pp. 1892-1906
    • Ku, N.O.1    Liao, J.2    Omary, M.B.3
  • 46
    • 33645290219 scopus 로고    scopus 로고
    • Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3
    • LeBron, C., Chen, L., Gilkes, D. M. and Chen, J. (2006) Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3. EMBO J. 25, 1196-1206
    • (2006) EMBO J , vol.25 , pp. 1196-1206
    • LeBron, C.1    Chen, L.2    Gilkes, D.M.3    Chen, J.4
  • 47
    • 0344628799 scopus 로고    scopus 로고
    • Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation
    • Zheng, W., Zhang, Z., Ganguly, S., Weller, J. L., Klein, D. C. and Cole, P. A. (2003) Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation. Nat. Struct. Biol. 10, 1054-1057
    • (2003) Nat. Struct. Biol , vol.10 , pp. 1054-1057
    • Zheng, W.1    Zhang, Z.2    Ganguly, S.3    Weller, J.L.4    Klein, D.C.5    Cole, P.A.6


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