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Volumn 465, Issue 1, 2015, Pages 53-58

Dopamine or biopterin deficiency potentiates phosphorylation at 40Ser and ubiquitination of tyrosine hydroxylase to be degraded by the ubiquitin proteasome system

Author keywords

Dopa responsive dystonia; Dopamine; Parkinson's disease; Proteasome; Tyrosine hydroxylase; Ubiquitin

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BIOPTERIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLOHEXIMIDE; DOPAMINE; DOPAMINE 2 RECEPTOR; PROTEASOME; SERINE; TETRAHYDROBIOPTERIN; TYROSINE 3 MONOOXYGENASE; UBIQUITIN; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; CYSTEINE PROTEINASE INHIBITOR; ISOQUINOLINE DERIVATIVE; LEUPEPTIN; N-(2-(4-BROMOCINNAMYLAMINO)ETHYL)-5-ISOQUINOLINESULFONAMIDE; SAPROPTERIN; SULFONAMIDE;

EID: 84940440623     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.07.125     Document Type: Article
Times cited : (30)

References (30)
  • 1
    • 9044252959 scopus 로고
    • Tyrosine hydroxylase. The initial step in norepinephrine biosynthesis
    • T. Nagatsu, M. Levitt, and S. Udenfriend Tyrosine hydroxylase. The initial step in norepinephrine biosynthesis J. Biol. Chem. 239 1964 2910 2917
    • (1964) J. Biol. Chem. , vol.239 , pp. 2910-2917
    • Nagatsu, T.1    Levitt, M.2    Udenfriend, S.3
  • 2
    • 0021905584 scopus 로고
    • A new mechanism for regulation of tyrosine 3-monooxygenase by end product and cyclic AMP-dependent protein kinase
    • S. Okuno, and H. Fujisawa A new mechanism for regulation of tyrosine 3-monooxygenase by end product and cyclic AMP-dependent protein kinase J. Biol. Chem. 260 1985 2633 2635
    • (1985) J. Biol. Chem. , vol.260 , pp. 2633-2635
    • Okuno, S.1    Fujisawa, H.2
  • 3
    • 0029810874 scopus 로고    scopus 로고
    • Conformational properties and stability of tyrosine hydroxylase studied by infrared spectroscopy. Effect of iron/catecholamine binding and phosphorylation
    • A. Martinez, J. Haavik, T. Flatmark, J.L. Arrondo, and A. Muga Conformational properties and stability of tyrosine hydroxylase studied by infrared spectroscopy. Effect of iron/catecholamine binding and phosphorylation J. Biol. Chem. 271 1996 19737 19742
    • (1996) J. Biol. Chem. , vol.271 , pp. 19737-19742
    • Martinez, A.1    Haavik, J.2    Flatmark, T.3    Arrondo, J.L.4    Muga, A.5
  • 4
    • 0033167087 scopus 로고    scopus 로고
    • Limited proteolysis of tyrosine hydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding
    • R.I. McCulloch, and P.F. Fitzpatrick Limited proteolysis of tyrosine hydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding Arch. Biochem. Biophys. 367 1999 143 145
    • (1999) Arch. Biochem. Biophys. , vol.367 , pp. 143-145
    • McCulloch, R.I.1    Fitzpatrick, P.F.2
  • 5
    • 0032560609 scopus 로고    scopus 로고
    • Effects of phosphorylation of serine 40 of tyrosine hydroxylase on binding of catecholamines: Evidence for a novel regulatory mechanism
    • A.J. Ramsey, and P.F. Fitzpatrick Effects of phosphorylation of serine 40 of tyrosine hydroxylase on binding of catecholamines: evidence for a novel regulatory mechanism Biochemistry 37 1998 8980 8986
    • (1998) Biochemistry , vol.37 , pp. 8980-8986
    • Ramsey, A.J.1    Fitzpatrick, P.F.2
  • 8
    • 38649121457 scopus 로고    scopus 로고
    • A brain-specific decrease of the tyrosine hydroxylase protein in sepiapterin reductase-null mice-as a mouse model for Parkinson's disease
    • C. Takazawa, K. Fujimoto, D. Homma, C. Sumi-Ichinose, T. Nomura, H. Ichinose, and S. Katoh A brain-specific decrease of the tyrosine hydroxylase protein in sepiapterin reductase-null mice-as a mouse model for Parkinson's disease Biochem. Biophys. Res. Commun. 367 2008 787 792
    • (2008) Biochem. Biophys. Res. Commun. , vol.367 , pp. 787-792
    • Takazawa, C.1    Fujimoto, K.2    Homma, D.3    Sumi-Ichinose, C.4    Nomura, T.5    Ichinose, H.6    Katoh, S.7
  • 11
    • 0028835506 scopus 로고
    • Striatal dihydroxyphenylalanine decarboxylase and tyrosine hydroxylase protein in idiopathic Parkinson's disease and dominantly inherited olivopontocerebellar atrophy
    • X.H. Zhong, J.W. Haycock, K. Shannak, Y. Robitaille, J. Fratkin, A.H. Koeppen, O. Hornykiewicz, and S.J. Kish Striatal dihydroxyphenylalanine decarboxylase and tyrosine hydroxylase protein in idiopathic Parkinson's disease and dominantly inherited olivopontocerebellar atrophy Mov. Disord. 10 1995 10 17
    • (1995) Mov. Disord. , vol.10 , pp. 10-17
    • Zhong, X.H.1    Haycock, J.W.2    Shannak, K.3    Robitaille, Y.4    Fratkin, J.5    Koeppen, A.H.6    Hornykiewicz, O.7    Kish, S.J.8
  • 14
    • 70949084763 scopus 로고    scopus 로고
    • Accumulation of phosphorylated tyrosine hydroxylase into insoluble protein aggregates by inhibition of an ubiquitin-proteasome system in PC12D cells
    • I. Kawahata, H. Tokuoka, H. Parvez, and H. Ichinose Accumulation of phosphorylated tyrosine hydroxylase into insoluble protein aggregates by inhibition of an ubiquitin-proteasome system in PC12D cells J. Neural Transm. 116 2009 1571 1578
    • (2009) J. Neural Transm. , vol.116 , pp. 1571-1578
    • Kawahata, I.1    Tokuoka, H.2    Parvez, H.3    Ichinose, H.4
  • 15
    • 18344365954 scopus 로고    scopus 로고
    • Ubiquitination of soluble and membrane-bound tyrosine hydroxylase and degradation of the soluble form
    • A.P. Doskeland, and T. Flatmark Ubiquitination of soluble and membrane-bound tyrosine hydroxylase and degradation of the soluble form Eur. J. Biochem. 269 2002 1561 1569
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1561-1569
    • Doskeland, A.P.1    Flatmark, T.2
  • 16
    • 79953729317 scopus 로고    scopus 로고
    • Phosphorylation of the N-terminal portion of tyrosine hydroxylase triggers proteasomal digestion of the enzyme
    • A. Nakashima, K. Mori, Y.S. Kaneko, N. Hayashi, T. Nagatsu, and A. Ota Phosphorylation of the N-terminal portion of tyrosine hydroxylase triggers proteasomal digestion of the enzyme Biochem. Biophys. Res. Commun. 407 2011 343 347
    • (2011) Biochem. Biophys. Res. Commun. , vol.407 , pp. 343-347
    • Nakashima, A.1    Mori, K.2    Kaneko, Y.S.3    Hayashi, N.4    Nagatsu, T.5    Ota, A.6
  • 17
    • 84923341917 scopus 로고    scopus 로고
    • Tyrosine hydroxylase is short-term regulated by the ubiquitin-proteasome system in PC12 cells and hypothalamic and brainstem neurons from spontaneously hypertensive rats: Possible implications in hypertension
    • N.A. Carbajosa, G. Corradi, M.A. Verrilli, M.J. Guil, M.S. Vatta, and M.M. Gironacci Tyrosine hydroxylase is short-term regulated by the ubiquitin-proteasome system in PC12 cells and hypothalamic and brainstem neurons from spontaneously hypertensive rats: possible implications in hypertension PLoS One 10 2015 e0116597
    • (2015) PLoS One , vol.10
    • Carbajosa, N.A.1    Corradi, G.2    Verrilli, M.A.3    Guil, M.J.4    Vatta, M.S.5    Gironacci, M.M.6
  • 18
    • 0023150860 scopus 로고
    • Neuritic growth from a new subline of PC12 pheochromocytoma cells: Cyclic AMP mimics the action of nerve growth factor
    • R. Katoh-Semba, S. Kitajima, Y. Yamazaki, and M. Sano Neuritic growth from a new subline of PC12 pheochromocytoma cells: cyclic AMP mimics the action of nerve growth factor J. Neurosci. Res. 17 1987 36 44
    • (1987) J. Neurosci. Res. , vol.17 , pp. 36-44
    • Katoh-Semba, R.1    Kitajima, S.2    Yamazaki, Y.3    Sano, M.4
  • 19
    • 77956228616 scopus 로고    scopus 로고
    • Reconstruction and quantitative evaluation of dopaminergic innervation of striatal neurons in dissociated primary cultures
    • S. Wakita, Y. Izumi, T. Matsuo, T. Kume, Y. Takada-Takatori, H. Sawada, and A. Akaike Reconstruction and quantitative evaluation of dopaminergic innervation of striatal neurons in dissociated primary cultures J. Neurosci. Methods 192 2010 83 89
    • (2010) J. Neurosci. Methods , vol.192 , pp. 83-89
    • Wakita, S.1    Izumi, Y.2    Matsuo, T.3    Kume, T.4    Takada-Takatori, Y.5    Sawada, H.6    Akaike, A.7
  • 20
    • 0020333428 scopus 로고
    • Stimulation of D2-dopamine receptors in rat neostriatum inhibits the release of acetylcholine and dopamine but does not affect the release of gamma-aminobutyric acid, glutamate or serotonin
    • J.C. Stoof, T. De Boer, P. Sminia, and A.H. Mulder Stimulation of D2-dopamine receptors in rat neostriatum inhibits the release of acetylcholine and dopamine but does not affect the release of gamma-aminobutyric acid, glutamate or serotonin Eur. J. Pharmacol. 84 1982 211 214
    • (1982) Eur. J. Pharmacol. , vol.84 , pp. 211-214
    • Stoof, J.C.1    De Boer, T.2    Sminia, P.3    Mulder, A.H.4
  • 21
    • 0026062464 scopus 로고
    • Dopaminergic regulation of dopamine release from PC12 cells via a pertussis toxin-sensitive G protein
    • N.D. Courtney, A.C. Howlett, and T.C. Westfall Dopaminergic regulation of dopamine release from PC12 cells via a pertussis toxin-sensitive G protein Neurosci. Lett. 122 1991 261 264
    • (1991) Neurosci. Lett. , vol.122 , pp. 261-264
    • Courtney, N.D.1    Howlett, A.C.2    Westfall, T.C.3
  • 22
    • 0030697293 scopus 로고    scopus 로고
    • Expression of dopamine D2 receptor in PC-12 cells and regulation of membrane conductances by dopamine
    • W.H. Zhu, L. Conforti, and D.E. Millhorn Expression of dopamine D2 receptor in PC-12 cells and regulation of membrane conductances by dopamine Am. J. Physiol. 273 1997 C1143 C1150
    • (1997) Am. J. Physiol. , vol.273 , pp. C1143-C1150
    • Zhu, W.H.1    Conforti, L.2    Millhorn, D.E.3
  • 23
    • 0032129190 scopus 로고    scopus 로고
    • D2-Like dopamine autoreceptor activation reduces quantal size in PC12 cells
    • E.N. Pothos, S. Przedborski, V. Davila, Y. Schmitz, and D. Sulzer D2-Like dopamine autoreceptor activation reduces quantal size in PC12 cells J. Neurosci. 18 1998 5575 5585
    • (1998) J. Neurosci. , vol.18 , pp. 5575-5585
    • Pothos, E.N.1    Przedborski, S.2    Davila, V.3    Schmitz, Y.4    Sulzer, D.5
  • 24
    • 57349095241 scopus 로고    scopus 로고
    • Dopamine D2 receptor expression is altered by changes in cellular iron levels in PC12 cells and rat brain tissue
    • E.L. Unger, J.A. Wiesinger, L. Hao, and J.L. Beard Dopamine D2 receptor expression is altered by changes in cellular iron levels in PC12 cells and rat brain tissue J. Nutr. 138 2008 2487 2494
    • (2008) J. Nutr. , vol.138 , pp. 2487-2494
    • Unger, E.L.1    Wiesinger, J.A.2    Hao, L.3    Beard, J.L.4
  • 25
    • 0023025693 scopus 로고
    • Identification of four phosphorylation sites in the N-terminal region of tyrosine hydroxylase
    • D.G. Campbell, D.G. Hardie, and P.R. Vulliet Identification of four phosphorylation sites in the N-terminal region of tyrosine hydroxylase J. Biol. Chem. 261 1986 10489 10492
    • (1986) J. Biol. Chem. , vol.261 , pp. 10489-10492
    • Campbell, D.G.1    Hardie, D.G.2    Vulliet, P.R.3
  • 26
    • 0024596455 scopus 로고
    • Mechanisms of signal transduction at the dopamine D2 receptor
    • L. Vallar, and J. Meldolesi Mechanisms of signal transduction at the dopamine D2 receptor Trends Pharmacol. Sci. 10 1989 74 77
    • (1989) Trends Pharmacol. Sci. , vol.10 , pp. 74-77
    • Vallar, L.1    Meldolesi, J.2
  • 27
    • 0028009971 scopus 로고
    • The stability of endogenous tyrosine hydroxylase protein in PC-12 cells differs from that expressed in mouse fibroblasts by gene transfer
    • D.K. Wu, and C.L. Cepko The stability of endogenous tyrosine hydroxylase protein in PC-12 cells differs from that expressed in mouse fibroblasts by gene transfer J. Neurochem. 62 1994 863 872
    • (1994) J. Neurochem. , vol.62 , pp. 863-872
    • Wu, D.K.1    Cepko, C.L.2
  • 28
    • 0023034890 scopus 로고
    • Induction of tyrosine hydroxylase by cyclic AMP and glucocorticoids in a rat pheochromocytoma cell line: Effect of the inducing agents alone or in combination on the enzyme levels and rate of synthesis of tyrosine hydroxylase
    • A.W. Tank, L. Ham, and P. Curella Induction of tyrosine hydroxylase by cyclic AMP and glucocorticoids in a rat pheochromocytoma cell line: effect of the inducing agents alone or in combination on the enzyme levels and rate of synthesis of tyrosine hydroxylase Mol. Pharmacol. 30 1986 486 496
    • (1986) Mol. Pharmacol. , vol.30 , pp. 486-496
    • Tank, A.W.1    Ham, L.2    Curella, P.3
  • 29
    • 2542510404 scopus 로고    scopus 로고
    • Protein synthesis blockade differentially affects the degradation of constitutive and nicotinic receptor-induced tyrosine hydroxylase protein level in isolated bovine chromaffin cells
    • E. Fernandez, and G.L. Craviso Protein synthesis blockade differentially affects the degradation of constitutive and nicotinic receptor-induced tyrosine hydroxylase protein level in isolated bovine chromaffin cells J. Neurochem. 73 1999 169 178
    • (1999) J. Neurochem. , vol.73 , pp. 169-178
    • Fernandez, E.1    Craviso, G.L.2
  • 30
    • 33846979780 scopus 로고    scopus 로고
    • Differential expression of the B'beta regulatory subunit of protein phosphatase 2A modulates tyrosine hydroxylase phosphorylation and catecholamine synthesis
    • A. Saraf, D.M. Virshup, and S. Strack Differential expression of the B'beta regulatory subunit of protein phosphatase 2A modulates tyrosine hydroxylase phosphorylation and catecholamine synthesis J. Biol. Chem. 282 2007 573 580
    • (2007) J. Biol. Chem. , vol.282 , pp. 573-580
    • Saraf, A.1    Virshup, D.M.2    Strack, S.3


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