Characterization of the sites phosphorylated on tyrosine hydroxylase by Ca2+ and phospholipid-dependent protein kinase, calmodulin-dependent multiprotein kinase and cyclic AMP-dependent protein kinase

Philip R Vulliet, James R. Woodgett, Stefano Ferrari, D. Grahame Hardie

Research output: Contribution to journalArticlepeer-review

74 Scopus citations

Abstract

Tyrosine hydroxylase purified from rat pheochromocytoma is phosphorylated rapidly by the Ca2+- and phospholipid-dependent protein kinase (protein kinase C) purified from rat or sheep brain. Phosphorylation was stimulated 14-fold by Ca2+ and phosphatidylserine and occurred at a rate comparable with that of the phosphorylation of histone H1. The phospholipid-dependent protein kinase phosphorylates a single site which is identical to that phosphorylated by cyclic AMP-dependent protein kinase and to the secondary site of phosphorylation by the calmodulin-dependent multiprotein kinase. The implications of these results with respect to the regulation of catecholamine biosynthesis in adrenal medulla are discussed.

Original languageEnglish (US)
Pages (from-to)335-339
Number of pages5
JournalFEBS Letters
Volume182
Issue number2
DOIs
StatePublished - Mar 25 1985
Externally publishedYes

Keywords

  • Acetylcholine
  • Calmodulin-dependent protein kinase
  • Cyclic AMP-depdent protein kinase
  • Phospholipid-dependent protein kinase
  • Phosphorylation
  • Tyrosine hydroxylase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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