Dimerization Activates the Epidermal Growth Factor Receptor Tyrosine Kinase

  • Marcel Spaargaren
  • Libert H. K. Defize
  • Johannes Boonstra
  • Siegfried W. de Laat
Conference paper
Part of the NATO ASI Series book series (volume 52)

Abstract

The epidermal growth factor receptor (EGF-R) is a transmembrane glycoprotein of 170 kDa with an extracellular ligand binding domain, a single hydrophobic transmembrane stretch, and an intracellular domain containing protein tyrosine kinase activity (Ullrich et al., 1984). Binding of EGF to its receptor enhances this tyrosine kinase activity, thus inducing tyrosine phosphorylation of several protein substrates including the EGF-R itself (Hunter and Cooper, 1985). Activation of the EGF-R tyrosine kinase results in a cascade of biochemical and physiological responses, finally leading to stimulation of DNA synthesis and cell division in most cells (Carpenter, 1987). Using EGF-R mutants, the protein tyrosine kinase activity was shown to be essential for mitogenic signaling (Schlessinger, 1988a).

Keywords

Tyrosine Electrophoresis Oligomerization Angiotensin Saponin 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1991

Authors and Affiliations

  • Marcel Spaargaren
    • 1
    • 2
  • Libert H. K. Defize
    • 1
  • Johannes Boonstra
    • 2
  • Siegfried W. de Laat
    • 1
  1. 1.Hubrecht LaboratoryNetherlands Institute for Developmental BiologyUtrechtThe Netherlands
  2. 2.Department of Molecular Cell BiologyUniversity of UtrechtUtrechtThe Netherlands

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