Ephrin-B1 (EFNB1)

Ephrin-B1 (EFNB1) is a transmembrane ligand protein for the Eph family of receptor tyrosine kinases, mediating bidirectional signaling that is critical for cell adhesion, tissue patterning, and neural development[1][5]. Expressed on the cell surface, Ephrin-B1 engages EphB receptors on adjacent cells, forming signal complexes that regulate various aspects of morphogenesis, craniofacial and neural development, and bone formation[1][3][5]. The protein's cytoplasmic tail mediates reverse signaling and interacts with PDZ domain-containing proteins such as PTPN13 and NHERF1, influencing cell cycle progression, osteoblast differentiation, and microtubule dynamics[2][3]. Pathogenic mutations in EFNB1 cause craniofrontonasal syndrome, affecting skull and facial development, and altered expression/function is implicated in certain cancers and therapeutic resistances[1][2][3][5]. Ephrin-B1 does not currently have approved direct pharmacological modulators but is of interest in oncology and regenerative medicine[2][3].

Other names

Ephrin-B1 C-terminal fragmentEphrin-B1 intracellular domainEFL3EPLG2LERK2ELK-LEphrin-B1 CTFEphrin-B1 ICDELK ligandEPH-related receptor tyrosine kinase ligand 2CFNDCFNSEFB1EFL-3

Modulation of cell sensitivity to anti-microtubule agents (such as paclitaxel) via microtubule interactions[2] Interference with Eph/ephrin signaling alters cell adhesion, proliferation, and migration[2][3] Reverse signaling through cytoplasmic domain following Eph receptor binding leads to downstream effects on differentiation and cell cycle[3]