Carboxy-terminal truncations of epidermal growth factor (EGF) receptor affect diverse EGF-induced cellular responses.

@article{Li1991CarboxyterminalTO,
  title={Carboxy-terminal truncations of epidermal growth factor (EGF) receptor affect diverse EGF-induced cellular responses.},
  author={Weiwei Li and Nashrudeen Hack and Ben L Margolis and Axel Ullrich and Karl L. Skorecki and Joseph Schlessinger},
  journal={Cell regulation},
  year={1991},
  volume={2 8},
  pages={
          641-9
        }
}
The binding of epidermal growth factor (EGF) to its receptor induces tyrosine phosphorylation of phospholipase C gamma (PLC gamma), which appears to be necessary for its activation leading to phosphatidyl inositol (PI) hydrolysis. Moreover, EGF-receptor (EGF-R) activation and autophosphorylation results in binding of PLC gamma to the tyrosine phosphorylated carboxy-terminus of the receptor. To gain further insights into the mechanisms and interactions regulating these processes, we have… CONTINUE READING

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