EGFR is a receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. The known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. The ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. EGFR activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. It may also activate the NF-kappa-B signaling cascade. EGFR also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. It also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. Endocytosis and inhibition of the activated EGFR by phosphatases like PTPRJ and PTPRK constitute immediate regulatory mechanisms. Upon EGF-binding EPS15 is phosphorylated and it regulates EGFR endocytosis and activity. Moreover, inducible feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative regulatory mechanisms for the EGFR signaling. EGFR also forms a heterodimer with ERBB2. EGFR is single-pass type I membrane protein of plasma membrane and many intracellular membranes. In response to EGF, EGFR is translocated from the cell membrane to the nucleus via Golgi and ER. EGFR undergo endocytosis upon activation by ligand. Isoform 2 is secreted. EGFR is ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers.

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