Epidermal Growth Factor (EGF) Receptor (EGFR, HER-1, c-ErbB-1) is a member of the Epidermal Growth Factor Receptor family of Receptor Tyrosine Kinases. These cell surface receptors play an important role in the flow of information from the outside of a cell to the inside. Upon binding of EGF to the extracellular domain, the receptor undergoes dimerization and becomes phosphorylated on several tyrosine residues within the cytoplasmic domain. These result in EGFR activation and increased tyrosine kinase activity toward a variety of intracellular substrates. Autophosphorylation of tyrosine 845, 992 and 1173 are critical to EGFR signaling. Phosphorylation at tyrosine 992 creates a direct binding site for phospholipase C-γ (PLC-γ) resulting in activation of protein kinase C and subsequent downstream signaling cascades. Phosphorylation at 1173 creates a major binding site for the protein tyrosine phosphatase SHP-1, which can dephosphorylate EGFR and thereby block EGFR-induced activation of the ERK1/2 signaling pathway. Tyrosine 845 phosphorylation is mediated by integrin engagement and Src, and regulates receptor function and tumor progression.
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