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. 1991 Feb;11(2):913-9.
doi: 10.1128/mcb.11.2.913-919.1991.

Epidermal growth factor (EGF) stimulates association and kinase activity of Raf-1 with the EGF receptor

H App  1 , R Hazan, A Zilberstein, A Ullrich, J Schlessinger, U Rapp
Affiliations

Epidermal growth factor (EGF) stimulates association and kinase activity of Raf-1 with the EGF receptor

H App et al. Mol Cell Biol. 1991 Feb.

Abstract

Raf-1 serine- and threonine-specific protein kinase is transiently activated in cells expressing the epidermal growth factor (EGF) receptor upon treatment with EGF. The stimulated EGF receptor coimmunoprecipitates with Raf-1 kinase and mediates protein kinase C-independent phosphorylation of Raf-1 on serine residues. Hyperphosphorylated Raf-1 has lower mobility on sodium dodecyl sulfate gels and has sixfold-increased activity in immunocomplex kinase assay with histone H1 or Raf-1 sequence-derived peptide as a substrate. Raf-1 activation requires kinase-active EGF receptor; a point mutant lacking tyrosine kinase activity in inactive in Raf-1 coupling and association. It is noteworthy that tyrosine phosphorylation of c-Raf-1 induced by EGF was not detected in these cells. These observations suggest that Raf-1 kinase may act as an important downstream effector of EGF signal transduction.

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