Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase

P. R. Vulliet, J. R. Woodgett, P. Cohen

    Research output: Contribution to journalArticle

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    Abstract

    Tyrosine hydroxylase purified from rat pheochromocytoma was phosphorylated stoichiometrically by either cyclic AMP-dependent protein kinase or calmodulin-dependent multiprotein kinase from skeletal muscle, but not by five other protein kinases tested. The activity of tyrosine hydroxylase was elevated 3-fold by cyclic AMP-dependent protein kinase, but no activation was observed after phosphorylation by calmodulin-dependent multiprotein kinase. Phosphorylation produced by cyclic AMP-dependent protein kinase and calmodulin-dependent multiprotein kinase was additive, suggesting different sites of phosphorylation. This was confirmed by high-performance liquid chromatography analysis of tryptic phosphopeptides which demonstrated that the major sites phosphorylated by each protein kinase was distinct. A calmodulin-dependent multiprotein kinase that had identical properties and substrate specificity to the skeletal muscle enzyme was partially purified from rat pheochromocytoma. The possibility that this protein kinase is involved in the regulation of tyrosine hydroxylase activity in adrenergic tissue in vivo is discussed.

    Original languageEnglish
    Pages (from-to)13680-13683
    Number of pages4
    JournalJournal of Biological Chemistry
    Volume259
    Issue number22
    Publication statusPublished - 1 Dec 1984

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    Calcium-Calmodulin-Dependent Protein Kinases
    Phosphorylation
    Tyrosine 3-Monooxygenase
    Cyclic AMP-Dependent Protein Kinases
    Protein Kinases
    Pheochromocytoma
    Muscle
    Rats
    Skeletal Muscle
    Phosphopeptides
    High performance liquid chromatography
    Substrate Specificity
    Adrenergic Agents
    Chemical activation
    High Pressure Liquid Chromatography
    Tissue
    Substrates
    Enzymes

    Cite this

    Vulliet, P. R. ; Woodgett, J. R. ; Cohen, P. / Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase. In: Journal of Biological Chemistry. 1984 ; Vol. 259, No. 22. pp. 13680-13683.
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    abstract = "Tyrosine hydroxylase purified from rat pheochromocytoma was phosphorylated stoichiometrically by either cyclic AMP-dependent protein kinase or calmodulin-dependent multiprotein kinase from skeletal muscle, but not by five other protein kinases tested. The activity of tyrosine hydroxylase was elevated 3-fold by cyclic AMP-dependent protein kinase, but no activation was observed after phosphorylation by calmodulin-dependent multiprotein kinase. Phosphorylation produced by cyclic AMP-dependent protein kinase and calmodulin-dependent multiprotein kinase was additive, suggesting different sites of phosphorylation. This was confirmed by high-performance liquid chromatography analysis of tryptic phosphopeptides which demonstrated that the major sites phosphorylated by each protein kinase was distinct. A calmodulin-dependent multiprotein kinase that had identical properties and substrate specificity to the skeletal muscle enzyme was partially purified from rat pheochromocytoma. The possibility that this protein kinase is involved in the regulation of tyrosine hydroxylase activity in adrenergic tissue in vivo is discussed.",
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    Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase. / Vulliet, P. R.; Woodgett, J. R.; Cohen, P.

    In: Journal of Biological Chemistry, Vol. 259, No. 22, 01.12.1984, p. 13680-13683.

    Research output: Contribution to journalArticle

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    T1 - Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase

    AU - Vulliet, P. R.

    AU - Woodgett, J. R.

    AU - Cohen, P.

    PY - 1984/12/1

    Y1 - 1984/12/1

    N2 - Tyrosine hydroxylase purified from rat pheochromocytoma was phosphorylated stoichiometrically by either cyclic AMP-dependent protein kinase or calmodulin-dependent multiprotein kinase from skeletal muscle, but not by five other protein kinases tested. The activity of tyrosine hydroxylase was elevated 3-fold by cyclic AMP-dependent protein kinase, but no activation was observed after phosphorylation by calmodulin-dependent multiprotein kinase. Phosphorylation produced by cyclic AMP-dependent protein kinase and calmodulin-dependent multiprotein kinase was additive, suggesting different sites of phosphorylation. This was confirmed by high-performance liquid chromatography analysis of tryptic phosphopeptides which demonstrated that the major sites phosphorylated by each protein kinase was distinct. A calmodulin-dependent multiprotein kinase that had identical properties and substrate specificity to the skeletal muscle enzyme was partially purified from rat pheochromocytoma. The possibility that this protein kinase is involved in the regulation of tyrosine hydroxylase activity in adrenergic tissue in vivo is discussed.

    AB - Tyrosine hydroxylase purified from rat pheochromocytoma was phosphorylated stoichiometrically by either cyclic AMP-dependent protein kinase or calmodulin-dependent multiprotein kinase from skeletal muscle, but not by five other protein kinases tested. The activity of tyrosine hydroxylase was elevated 3-fold by cyclic AMP-dependent protein kinase, but no activation was observed after phosphorylation by calmodulin-dependent multiprotein kinase. Phosphorylation produced by cyclic AMP-dependent protein kinase and calmodulin-dependent multiprotein kinase was additive, suggesting different sites of phosphorylation. This was confirmed by high-performance liquid chromatography analysis of tryptic phosphopeptides which demonstrated that the major sites phosphorylated by each protein kinase was distinct. A calmodulin-dependent multiprotein kinase that had identical properties and substrate specificity to the skeletal muscle enzyme was partially purified from rat pheochromocytoma. The possibility that this protein kinase is involved in the regulation of tyrosine hydroxylase activity in adrenergic tissue in vivo is discussed.

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