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).
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Spaargaren, M., Defize, L.H.K., Boonstra, J., de Laat, S.W. (1991). Dimerization Activates the Epidermal Growth Factor Receptor Tyrosine Kinase. In: Ross, E.M., Wirtz, K.W.A. (eds) Biological Signal Transduction. NATO ASI Series, vol 52. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75136-3_4
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DOI: https://doi.org/10.1007/978-3-642-75136-3_4
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