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.
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.
Vulliet
P R
PR
Woodgett
J R
JR
Ferrari
S
S
Hardie
D G
DG
D000818:Animals; D001921:Brain / Q000201:enzymology; D002118:Calcium / Q000494:pharmacology; D002147:Calmodulin / Q000494:pharmacology*; D000242:Cyclic AMP / Q000494:pharmacology*; D007525:Isoelectric Focusing; D010446:Peptide Fragments / Q000378:metabolism; D010673:Pheochromocytoma / Q000201:enzymology; D010718:Phosphatidylserines / Q000494:pharmacology; D010766:Phosphorylation; D011493:Protein Kinase C; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D012756:Sheep; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism*
D002147:Calmodulin; D010446:Peptide Fragments; D010718:Phosphatidylserines; D000242:Cyclic AMP; D014446:Tyrosine 3-Monooxygenase; D011494:Protein Kinases; D011493:Protein Kinase C; D002118:Calcium