Receptor Family

Eph receptors: bidirectional signalling molecules with cell adhesion properties Eph receptors have a large extracellular domain with a cysteine-rich region that is involved in disulfide bond formation, followed by two fibronectin type III repeats. The ligands for these receptors are ephrins. Unlike most RTK ligands, ephrins require membrane attachment, and therefore cell-cell interaction, to activate their receptors. Ephrin A ligands are attached by glycosylphosphatidylinositol(GPI) linkage, whereas ephrin B ligands are transmembrane proteins. Upon binding to their receptors, ephrin B ligands can be tyrosine phosphorylated in their intracellular domain that evokes signal transduction within the ligand-containing cell. Thus, individual ephrins and Eph receptors can participate as both a ligand and a receptor, a phenomenon known as bidirectional signalling. Eph receptors and ephrins have emerged as key regulators in the repulsion and adhesion of cells. They are important in morphogenesis, specifically in the boundary demarcation of tissues such as in rhombomere formation and axonal guidance. Ephrin-A/EphA receptor signalling plays a key role in controlling the size of the mouse cerebral cortex by regulating cortical progenitor cell apoptosis (Depaepe et al. 2005). Most human colorectal cancers lose expression of EphB at the adenoma−carcinoma transition. Loss of EphB expression strongly correlates with degree of malignancy. Reduction of EphB activity accelerates tumorigenesis in the colon and rectum of ApcMin/+ mice, and results in the formation of aggressive adenocarcinomas (Batlle et al. 2005).
Relevant reviews and publications:
12100883, 10851175, 10600686, 11248553, 11440711, 11466320, 11128993, 10730216, 10958785
no tree for this subfamily