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Background
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Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The ligand-activated form of EphB2, which belongs to the Tyr family of protein kinases, interacts with multiple proteins, including GTPase-activating protein (RASGAP) through its SH2 domain. It binds RASGAP through the juxtamembrane tyrosines residues, and also interacts with PRKCABP and GRIP1 This type I membrane protein is expressed in brain, heart, lung, kidney, placenta, pancreas, liver and skeletal muscle. It is preferentially expressed in fetal brain. This protein contains putatively 2 fibronectin type III domains and 1 sterile alpha motif (SAM) domain.
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Background
References
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- Thanos, C.D., et al., Science 283(5403):833-836 (1999).
- Tang, X.X., et al., Oncogene 17(4):521-526 (1998).
- Fox, G.M., et al., Oncogene 10(5):897-905 (1995).
- Ikegaki, N., et al., Hum. Mol. Genet. 4(11):2033-2045 (1995).
- Iwase, T., et al., Biochem. Biophys. Res. Commun. 194(2):698-705 (1993).
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