Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase

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

Research output: Contribution to journalArticle

115 Scopus citations

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 (US)
Pages (from-to)13680-13683
Number of pages4
JournalJournal of Biological Chemistry
Volume259
Issue number22
StatePublished - 1984
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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