This gene encodes a member of the epidermal growth factor superfamily. The encoded protein is synthesized as a large precursor molecule that is proteolytically cleaved to generate the 53-amino acid epidermal growth factor peptide. This protein acts a potent mitogenic factor that plays an important role in the growth, proliferation and differentiation of numerous cell types. This protein acts by binding the high affinity cell surface receptor, epidermal growth factor receptor. Defects in this gene are the cause of hypomagnesemia type 4. Dysregulation of this gene has been associated with the growth and progression of certain cancers. Alternate splicing results in multiple transcript variants
EGFR is a transmembrane glycoprotein that is a member of the protein kinase superfamily. This protein is a receptor for members of the epidermal growth factor family. EGFR is a cell surface protein that binds to epidermal growth factor. Binding of the protein to a ligand induces receptor dimerization and tyrosine autophosphorylation and leads to cell proliferation. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK; PI3 kinase-AKT; PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. 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.
As a member of the epidermal growth factor receptor (EGFR) family; EGFR protein is type I transmembrane glycoprotein that binds a subset of EGF family ligands including EGF; amphiregulin; TGF-α; betacellulin; etc. EGFR protein plays a crucial role in signaling pathway in the regulation of cell proliferation; survival and differentiation. Binding of a ligand induces EGFR protein homo- or heterodimerization; the subsequent tyrosine autophosphorylation and initiates various down stream pathways (MAPK; PI3K/PKB and STAT). In addition; EGFR signaling also has been shown to exert action on carcinogenesis and disease progression; and thus EGFR protein is proposed as a target for cancer therapy currently.
The EGFR subfamily of receptor tyrosine kinases is composed of EGFR; ErbB2; ErbB3 and ErbB4. The EGFR shares 43% - 44% aa sequence identity with the ECD of human EGFR subfamily. All these family members are type I transmembrane glycoproteins with an extracellular ligand binding domain. The extracellular ligand binding domain is containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a membrane-proximal tyrosine kinase domain. Ligand binding could induce EGFR homodimerization and heterodimerization with ErbB2; resulting in cell signaling; heterodimerization tyrosine phosphorylation and kinase activation. It can bind EGF; amphiregulin; TGF-alpha; betacellulin; epiregulin; HB-EGF; epigen; and so on. Its signaling regulates multiple biological functions including cell proliferation; differentiation; motility; and apoptosis. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR is overexpressed in different tumors. Several anti-cancer drugs use EGFR as target.
The EGFR subfamily of receptor tyrosine kinases is composed of EGFR, ErbB2, ErbB3 and ErbB4. The EGFR shares 43%-44% aa sequence identity with the ECD of human EGFR subfamily. All these family members are type I transmembrane glycoproteins with an extracellular ligand binding domain. The extracellular ligand binding domain is containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a membrane-proximal tyrosine kinase domain. Ligand binding could induce EGFR homodimerization and heterodimerization with ErbB2, resulting in cell signaling, heterodimerization tyrosine phosphorylation and kinase activation. It can bind EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, HB-EGF, epigen, and so on. Its signaling regulates multiple biological functions including cell proliferation, differentiation, motility, and apoptosis. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR is overexpressed in different tumors. Several anti-cancer drugs use EGFR as target.
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