EGFR Protein, Human (Active, 327a.a, sf9)

The EGFR protein, a receptor tyrosine kinase, binds ligands of the EGF family, including EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG, and HBEGF/heparin-binding EGF. This interaction initiates cascades that convert extracellular signals into cellular responses, involving receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2, activating downstream signaling cascades, including RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC, and STATs modules. Additionally, EGFR may trigger the NF-kappa-B signaling cascade and directly phosphorylate proteins like RGS16, activating its GTPase activity, potentially linking EGF receptor signaling to G protein-coupled receptor signaling. Furthermore, EGFR phosphorylates MUC1, enhancing its interaction with SRC and CTNNB1/beta-catenin. It positively regulates cell migration through interaction with CCDC88A/GIV, retaining EGFR at the cell membrane post-ligand stimulation, thereby promoting EGFR signaling and triggering cell migration. Beyond its canonical functions, EGFR contributes to enhancing learning and memory performance and plays a role in mammalian pain signaling, with isoform 2 potentially acting as an antagonist to EGF action.