Polycation-dependent, Ca2+-antagonized phosphorylation of calmodulin by casein kinase-2 and a spleen tyrosine protein kinase.
Ten distinct protein kinases have been tested for their ability to phosphorylate calmodulin. Only casein kinase-2 and a spleen tyrosine protein kinase (TPK-III) proved effective, their phosphorylation efficiency being dramatically enhanced by histones and other polybasic peptides while being depressed by 50 microM Ca2+. Phosphorylation by CK-2 takes place with ... a Km of 12 microM calmodulin, leading to the incorporation of more than 1.5 mol P/mol substrate. Ser81 and Thr79 are among the residues affected. On the other hand, the two tyrosyl residues of calmodulin are both phosphorylated by TPK-III, Tyr99 being preferred over Tyr138.
Mesh Terms:
Animals, Calcium, Calmodulin, Casein Kinases, Phosphorylation, Protein Kinase Inhibitors, Protein Kinases, Protein-Tyrosine Kinases, Rats, Spleen, Time Factors
Animals, Calcium, Calmodulin, Casein Kinases, Phosphorylation, Protein Kinase Inhibitors, Protein Kinases, Protein-Tyrosine Kinases, Rats, Spleen, Time Factors
FEBS Lett.
Date: May. 11, 1987
PubMed ID: 3472906
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