Epidermal growth factor receptor (EGFR) is a cell-membrane receptor tyrosine kinase belonging to the EGF-family of receptors, which binds a variety of extracellular protein ligands, including epidermal growth factor and transforming growth factor-alpha. Upon ligand-binding, two monomeric EGFR molecules bind together to form a homodimer, which gets activated by autophosphorylation. Following activation, the receptor dimer complex proceeds to phosphorylate cytoplasmic substrates, initiating a signaling cascade that drives many cellular responses, including changes in gene expression, cytoskeletal rearrangement, anti-apoptosis, and increased cell proliferation. Incidentally, EGFR can also pair with any other member of the EGF-family of receptors to form a heterodimer.
Due to its central role in processes such as cell division, mutations in the EGFR gene that result in a constitutive production of the protein tend to cause uncontrolled cell proliferation. EGFR mutations have been associated with different types of cancers, most notably epithelial cancers. About 30% of human primary tumors show an over-expression of EGFR, and this over-expression has also been significantly associated with disease stage, prognosis, survival, and response to chemotherapy. Of late, EGFR has been recognized as a suitable target for cancer therapy.