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

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...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 1985-01, Vol.182 (2), p.335-339
Main Authors: Vulliet, P.Richard, Woodgett, James R., Ferrari, Stefano, Hardie, D.Grahame
Format: Article
Language:English
Subjects:
Acetylcholine
Calmodulin-dependent protein kinase
Cyclic AMP-depdent protein kinase
Phospholipid-dependent protein kinase
Phosphorylation
Tyrosine hydroxylase
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(85)80328-8