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  • Title: 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.
    Author: Vulliet PR, Woodgett JR, Ferrari S, Hardie DG.
    Journal: FEBS Lett; 1985 Mar 25; 182(2):335-9. PubMed ID: 2858405.
    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 Hl. 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.
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