Phosphorylation of calmodulin by permeabilized fibroblasts overexpressing the human epidermal growth factor receptor.

@article{Frutos1997PhosphorylationOC,
  title={Phosphorylation of calmodulin by permeabilized fibroblasts overexpressing the human epidermal growth factor receptor.},
  author={Trinidad de Frutos and Jos{\'e} Mart{\'i}n-Nieto and Antonio Villalobo},
  journal={Biological chemistry},
  year={1997},
  volume={378 1},
  pages={31-7}
}
Detergent-permeabilized EGFR-T17 fibroblasts, which overexpress the human epidermal growth factor (EGF) receptor, phosphorylate both poly-L-(glutamic acid, tyrosine) and exogenous calmodulin in an EGF-stimulated manner. Phosphorylation of calmodulin requires the presence of cationic polypeptides, such as poly-L-(lysine) or histones, which exert a biphasic effect toward calmodulin phosphorylation. Optimum cationic polypeptide/calmodulin molar ratios of 0.3 and 7 were determined for poly-L… CONTINUE READING