EPH receptor A2 (ephrin type-A receptor 2) (EphA2)

EPH receptor A2 is a transmembrane glycoprotein belonging to the largest subfamily of human protein tyrosine kinases—the ephrin receptors. It consists of an extracellular region containing cysteine-rich domains and fibronectin type III repeats that bind membrane-bound ephrin-A ligands. Upon ligand binding, it activates intracellular phosphorylation cascades regulating diverse biological processes such as axon guidance during neural development, angiogenesis, cell migration, proliferation, and survival. In pathology, it plays roles in cancer progression/metastasis—where its overexpression often correlates with aggressive disease—and mediates cellular entry for several viruses including hepatitis C virus and Kaposi’s sarcoma-associated herpesvirus. Mutations are linked to inherited cataracts. Its complex biology makes it both a promising therapeutic target and a challenging one due to its involvement in essential physiological functions across multiple tissues.

Other names

Ephrin type-A receptor 2Epithelial cell kinase (ECK)Tyrosine-protein kinase receptor ECKTyrosine-protein kinase receptor MPK-5Tyrosine-protein kinase receptor SEK-2Myk 2Sek-2

Drugs may act by: - Inhibiting the tyrosine kinase activity to block downstream signaling pathways involved in cancer cell proliferation or survival. - Blocking ligand binding to prevent activation by ephrin-A ligands. - Preventing viral entry by interfering with virus-receptor interactions on host cells.