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. 1990 Feb;10(2):435–441. doi: 10.1128/mcb.10.2.435

Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor.

B Margolis 1, F Bellot 1, A M Honegger 1, A Ullrich 1, J Schlessinger 1, A Zilberstein 1
PMCID: PMC360807  PMID: 2153914

Abstract

Epidermal growth factor (EGF) treatment of NIH 3T3 cells transfected with wild-type EGF receptor induced tyrosine phosphorylation of phospholipase C-gamma (PLC-gamma). The EGF receptor and PLC-gamma were found to be physically associated such that antibodies directed against PLC-gamma or the EGF receptor coimmunoprecipitated both proteins. The association between PLC-gamma and wild-type EGF receptor was dependent on the concentration of EGF, but EGF did not enhance the association between PLC-gamma and a kinase-negative mutant of the EGF receptor. Oligomerization of the EGF receptor was not sufficient to induce association of the EGF receptor with PLC-gamma, since the kinase-negative mutant receptor underwent normal dimerization in response to EGF yet did not associate with PLC-gamma. The form of PLC-gamma associated with the EGF receptor appeared to be primarily the non-tyrosine-phosphorylated form. It is concluded that the kinase activity of the EGF receptor is essential for association of PLC-gamma with the EGF receptor, possibly by stimulating receptor autophosphorylation.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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