Biology:EPH receptor B1

Generic protein structure example

Ephrin type-B receptor 1 is a protein that in humans is encoded by the EPHB1 gene.

Function

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 protein encoded by this gene is a receptor for ephrin-B family members.

Interactions

EPH receptor B1 has been shown to interact with:

• ACP1
• GRB7 and
• NCK1
• Ephrin-B2

Further reading

• "The ephrins and Eph receptors in neural development". Annu. Rev. Neurosci. 21: 309–45. 1998. doi:10.1146/annurev.neuro.21.1.309. PMID 9530499. 
• "The Eph family receptors and ligands". Pharmacol. Ther. 77 (3): 151–81. 1998. doi:10.1016/S0163-7258(97)00112-5. PMID 9576626. 
• "Origins and formation of microvasculature in the developing kidney". Kidney Int. Suppl. 67: S7-11. 1998. doi:10.1046/j.1523-1755.1998.06702.x. PMID 9736245. 
• "Eph receptors and ephrins: effectors of morphogenesis". Development 126 (10): 2033–44. 1999. doi:10.1242/dev.126.10.2033. PMID 10207129. 
• "Eph receptors and ephrins: regulators of guidance and assembly". Int. Rev. Cytol.. International Review of Cytology 196: 177–244. 2000. doi:10.1016/S0074-7696(00)96005-4. ISBN 9780123646002. PMID 10730216. 
• "Roles of Eph receptors and ephrins in segmental patterning". Philos. Trans. R. Soc. Lond. B Biol. Sci. 355 (1399): 993–1002. 2000. doi:10.1098/rstb.2000.0635. PMID 11128993. 
• "Multiple roles of EPH receptors and ephrins in neural development". Nat. Rev. Neurosci. 2 (3): 155–64. 2001. doi:10.1038/35058515. PMID 11256076. 
• "Identification of residues in the beta platelet-derived growth factor receptor that confer specificity for binding to phospholipase C-gamma 1". Oncogene 8 (9): 2493–9. 1993. PMID 7689724. 
• "Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity". Science 266 (5186): 816–9. 1994. doi:10.1126/science.7973638. PMID 7973638. Bibcode: 1994Sci...266..816D. 
• "Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors". EMBO J. 13 (16): 3757–62. 1994. doi:10.1002/j.1460-2075.1994.tb06685.x. PMID 8070404. 
• "Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases". Mol. Immunol. 32 (16): 1197–205. 1995. doi:10.1016/0161-5890(95)00108-5. PMID 8559144. https://zenodo.org/record/1258339. 
• "Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis". Neuron 17 (1): 9–19. 1996. doi:10.1016/S0896-6273(00)80276-7. PMID 8755474. 
• "Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells". J. Biol. Chem. 271 (38): 23588–93. 1996. doi:10.1074/jbc.271.38.23588. PMID 8798570. 
• "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. 1996. doi:10.1101/gr.6.9.791. PMID 8889548. 
• "LERK-7: a ligand of the Eph-related kinases is developmentally regulated in the brain". Cytokine 9 (8): 540–9. 1997. doi:10.1006/cyto.1997.0199. PMID 9245480. 
• "Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee". Cell 90 (3): 403–4. 1997. doi:10.1016/S0092-8674(00)80500-0. PMID 9267020. 
• "Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase". J. Biol. Chem. 273 (3): 1303–8. 1998. doi:10.1074/jbc.273.3.1303. PMID 9430661. 
• "Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses". Genes Dev. 12 (5): 667–78. 1998. doi:10.1101/gad.12.5.667. PMID 9499402.