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Characterization of the sites phosphorylated on tyrosine hydroxylase by Ca 2+ and phospholipid‐dependent protein kinase, calmodulin‐dependent multiprotein kinase and cyclic AMP‐dependent protein kinase
Author(s) -
Vulliet P.Richard,
Woodgett James R.,
Ferrari Stefano,
Hardie D.Grahame
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80328-8
Subject(s) - protein kinase a , mitogen activated protein kinase kinase , chemistry , map2k7 , cyclin dependent kinase 2 , map kinase kinase kinase , biochemistry , cyclin dependent kinase 9 , calmodulin , phosphorylation , enzyme
Tyrosine hydroxylase purified from rat pheochromocytoma is phosphorylated rapidly by the Ca 2+ ‐ and phospholipid‐dependent protein kinase (protein kinase C) purified from rat or sheep brain. Phosphorylation was stimulated 14‐fold by Ca 2+ 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.