Insulin-stimulated phosphorylation of calmodulin.

  title={Insulin-stimulated phosphorylation of calmodulin.},
  author={D. Sacks and H. Davis and D. Crimmins and J. McDonald},
  journal={The Biochemical journal},
  volume={286 ( Pt 1)},
Calmodulin is phosphorylated in vitro by the insulin-receptor tyrosine kinase and a variety of serine/threonine kinases. Here we report that insulin stimulates the phosphorylation of calmodulin on average 3-fold in intact rat hepatocytes. Although calmodulin is constitutively phosphorylated, insulin increases phosphate incorporation into serine, threonine and tyrosine residues. We demonstrate that casein kinase II, an insulin-sensitive kinase, phosphorylates calmodulin in vitro on serine… Expand
Insulin-dependent phosphorylation of calmodulin in rat hepatocytes.
Phosphorylation of calmodulin
Phosphorylation of calmodulin. Functional implications.
Phosphorylation of calmodulin by Ca2+/calmodulin-dependent protein kinase IV.
Alteration of calmodulin-protein interactions by a monoclonal antibody to calmodulin.
  • D. Sacks
  • Biology, Medicine
  • Biochimica et biophysica acta
  • 1994
Tyrosine phosphorylation modulates the interaction of calmodulin with its target proteins.