Epidermal growth factor receptor (EGFR) is a 175 kDa transmembrane glycoprotein receptor tyrosine kinase that is involved in diverse cellular functions including cell proliferation, differentiation, motility, survival and in tissue development (1, 2). EGFR is regulated by EGF-stimulated autophosphorylation and by phorbol ester-stimulated, protein kinase C (Ca2+/ phospholipid-dependent enzyme) mediated phosphorylation at identified sites. EGFR contains additional phosphorylation sites including a prominent phosphothreonine and several phosphoserines which account for the majority of phosphate covalently bound to the receptor in vivo. Analysis of predicted secondary structure of EGFR reveals that all of the phosphorylation sites are located near beta turns (3).
Cytokine-cytokine receptor interaction
Delta-Notch Signaling Pathway
EGFR1 Signaling Pathway
MAPK signaling pathway
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