Phospho-EGFR (Py1086)

Epidermal growth factor receptor (EGFR) is a 170 kDa transmembrane glycoprotein receptor tyrosine kinase that, activated by epidermal growth factor (EGF), affects cell growth and differentiation (1). Binding of EGF or TGF alpha to EGFR activates tyrosine kinase activity of the receptor (2). The carboxy terminal tyrosine residues on EGFR, Tyr 1068, Tyr 1148, and Tyr 1173, are the major sites of autophosphorylation, which occurs as a result of EGF binding (3). Once activated, EGFR phosphotyrosines Y-1068 and Y-1173 mediate the binding of Grb2 to the EGFR. Another autophosphorylation site, Tyr 1086, is situated within the cytoplasmic domain, and is phosphorylated to a higher extent by c-Src than by EGFR (4).