Polycation‐dependent, Ca2+‐antagonized phosphorylation of calmodulin by casein kinase‐2 and a spleen tyrosine protein kinase

@article{Meggio1987PolycationdependentCP,
  title={Polycation‐dependent, Ca2+‐antagonized phosphorylation of calmodulin by casein kinase‐2 and a spleen tyrosine protein kinase},
  author={Flavio Meggio and Anna Maria Brunati and Lorenzo A. Pinna},
  journal={FEBS Letters},
  year={1987},
  volume={215}
}
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 μM Ca2+. Phosphorylation by CK‐2 takes place with a Km of 12 μM calmodulin, leading to the incorporation of more than 1.5 mol P/mol substrate. Ser81 and Thr79 are among the residues affected… Expand
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  • M. Kubo, C. Strott
  • Biology, Medicine
  • Biochemical and biophysical research communications
  • 1988
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