The epidermal growth factor receptor (EGFR) is a 170-kDa membrane bound receptor consisting of an extracellular ligand-binding domain, a single hydrophobic transmembrane region, and a tyrosine kinase domain-containing cytoplasmic region. Ligand binding induces receptor homo- or heterodimerization, triggering autophosphorylation of cytoplasmic tyrosine residues that provide docking sites for Src homology 2 (SH2) domain-containing signaling molecules. Src-mediated phosphorylation of EGFR at Tyr845 may contribute to EGFR hyperactivity in cancer, while autophosphorylation of EGFR at Tyr1068 and/or Tyr1173 in response to ligand binding is known to recruit cofactors (e.g. SHP1, RasGAP, SOS1, Grb2) that activate pathways associated with cell growth, apoptosis, adhesion, receptor endocytosis, and protein degradation.
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Regulatory Status |
RUO – Research Use Only |
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