EPHA2 (EPH receptor A2) is a receptor tyrosine kinase functioning as a multifaceted signaling hub in cancer biology and viral pathogenesis. Canonically, EPHA2 regulates cell migration, focal adhesion assembly, and growth factor signaling through ephrin-dependent mechanisms 1. Beyond classical ephrin signaling, EPHA2 acts as a viral entry receptor for both Epstein-Barr virus and cytomegalovirus in epithelial cells, interacting with viral glycoproteins gH/gL and gB to facilitate internalization 2. In glioblastoma, EPHA2 mediates platelet-derived growth factor A (PDGFA) activity independently of PDGFRA, contributing to malignant progression and therapeutic resistance 3. EPHA2 oncogenic activity extends across multiple cancer types through diverse mechanisms: m6A-methylated EPHA2 promotes vasculogenic mimicry in colorectal cancer via PI3K/AKT and ERK1/2 signaling 1; EPHA2 interaction with claudin-1 enhances cancer stemness and chemoresistance through AKT-CD44 axis activation 4; and hypoxia-induced TGFBI stabilizes EPHA2 protein to maintain glioma stem cell properties 5. In hepatic fibrosis, EPHA2/FAK/Src signaling regulates stellate cell glycolysis and activation 6. EPHA2 overexpression associates with poor prognosis across malignancies 7. Therapeutic strategies include dual EPHA2/PDGFRA inhibition, bicyclic peptide-based radiotheranostics 8, and emerging proteolysis-targeting chimera approaches 7.