Phosphorylation of tyrosine hydroxylase by cyclic GMP - Dependent protein kinase

R. Roskoski, Philip R Vulliet, D. B. Glass

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

Tyrosine hydroxylase purified from rat pheochromycytoma was phosphorylated and activated by purified cyclic GMP-dependent protein kinase as well as by cyclic AMP-dependent protein kinase catalytic subunit. The extent of activation was correlated with the degree of phosphate incorporated into the enzyme. Comparable stoichiometric ratios (0.6 mol phosphate/mol tyrosine hydroxylase subunit) were obtained at maximal concentrations of either cyclic AMP-dependent or cyclic GMP-dependent protein kinases. The enzymes appeared to mediate the phosphorylation of the same residue based on the observation that incorporation was not increased when both enzymes were present. The major tryptic phosphopeptide obtained from tyrosine hydroxylase phosphorylated by each protein kinase exhibited an identical retention time following HPLC. The purified phosphopeptides also exhibited identified isoelectric points. These data provide support for the notion that the protein kinases are phosphorylating the same residue of tyrosine hydroxylase.

Original languageEnglish (US)
Pages (from-to)840-845
Number of pages6
JournalJournal of Neurochemistry
Volume48
Issue number3
StatePublished - 1987
Externally publishedYes

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Cyclic GMP-Dependent Protein Kinases
Phosphorylation
Tyrosine 3-Monooxygenase
Phosphopeptides
Protein Kinases
Enzymes
Phosphates
Cyclic AMP-Dependent Protein Kinase Catalytic Subunits
Isoelectric Point
Cyclic AMP
Rats
Chemical activation
High Pressure Liquid Chromatography

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Phosphorylation of tyrosine hydroxylase by cyclic GMP - Dependent protein kinase. / Roskoski, R.; Vulliet, Philip R; Glass, D. B.

In: Journal of Neurochemistry, Vol. 48, No. 3, 1987, p. 840-845.

Research output: Contribution to journalArticle

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AB - Tyrosine hydroxylase purified from rat pheochromycytoma was phosphorylated and activated by purified cyclic GMP-dependent protein kinase as well as by cyclic AMP-dependent protein kinase catalytic subunit. The extent of activation was correlated with the degree of phosphate incorporated into the enzyme. Comparable stoichiometric ratios (0.6 mol phosphate/mol tyrosine hydroxylase subunit) were obtained at maximal concentrations of either cyclic AMP-dependent or cyclic GMP-dependent protein kinases. The enzymes appeared to mediate the phosphorylation of the same residue based on the observation that incorporation was not increased when both enzymes were present. The major tryptic phosphopeptide obtained from tyrosine hydroxylase phosphorylated by each protein kinase exhibited an identical retention time following HPLC. The purified phosphopeptides also exhibited identified isoelectric points. These data provide support for the notion that the protein kinases are phosphorylating the same residue of tyrosine hydroxylase.

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