Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase.

@article{Benguria1994PhosphorylationOC,
  title={Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase.},
  author={Alberto Benguria and Octavio Hern{\'a}ndez-Perera and Mar{\'i}a Teresa Mart{\'i}nez-Pastor and David B Sacks and Antonio Villalobo},
  journal={European journal of biochemistry},
  year={1994},
  volume={224 3},
  pages={909-16}
}
An epidermal-growth-factor(EGF)-receptor preparation isolated by calmodulin-affinity chromatography from rat liver plasma membranes is able to phosphorylate calmodulin. Calmodulin phosphorylation was enhanced 3-8-fold by EGF, was dependent on the presence of a polycation or basic protein and was inhibited by micromolar concentrations of Ca2+. Phosphate incorporation into calmodulin occurs predominantly on tyrosine residues. Partial proteolysis of phosphocalmodulin by thrombin identifies Tyr99… CONTINUE READING

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