Characterization of the sites phosphorylated on tyrosine hydroxylase by Ca super(2+) and phospholipid-dependent protein kinase, calmodulin-dependent multiprotein kinase and cyclic AMP-dependent protein kinase

Tyrosine hydroxylase purified from rat pheochromocytoma is phosphorylated rapidly by the Ca super(2+)-and phospholipid-dependent protein kinase (protein kinase C) purified from rat or sheep brain. Phosphorylation was simulated 14-fold by Ca super(2+) and phosphatidylserine and occurred at a rate com...

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Bibliographic Details
Published in:FEBS letters 1985-01, Vol.182 (2), p.335-339
Main Authors: Vulliet, PR, Woodgett, J R, Ferrari, S, Hardie, D G
Format: Article
Language:English
Subjects:
brain
calcium
phosphorylation
protein kinase
rats
tyrosine hydroxylase
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Summary:Tyrosine hydroxylase purified from rat pheochromocytoma is phosphorylated rapidly by the Ca super(2+)-and phospholipid-dependent protein kinase (protein kinase C) purified from rat or sheep brain. Phosphorylation was simulated 14-fold by Ca super(2+) 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 the phosphorylated by cyclic AMP-dependent protein kinase and to the secondary site of phosphorylation by the calmodulin-dependent multiprotein kinase. The implications of the results with respect to the regulation of catecholamine biosynthesis in adrenal medulla are discussed.
ISSN:0014-5793