C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity.

@article{Cochet1984CkinasePT,
  title={C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity.},
  author={Claude Cochet and Gordon N. Gill and Jill Meisenhelder and Jonathan A Cooper and Tony Hunter},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 4},
  pages={2553-8}
}
The Ca2+- and phospholipid-dependent protein kinase (C-kinase) binds tightly in the presence of Ca2+ to purified membranes of A431 human epidermoid carcinoma cells. The major membrane substrate for C-kinase is the epidermal growth factor (EGF) receptor. Phosphorylation of the EGF receptor is Ca2+-dependent and occurs at threonine and serine residues. After tryptic digestion of the receptor, three major phosphothreonine-containing peptides were identified. These are identical with three new… CONTINUE READING

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