EPHB3
{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
Ephrin type-B receptor 3 is a protein that in humans is encoded by the EPHB3 gene.{{cite journal | vauthors = Böhme B, Holtrich U, Wolf G, Luzius H, Grzeschik KH, Strebhardt K, Rübsamen-Waigmann H | title = PCR mediated detection of a new human receptor-tyrosine-kinase, HEK 2 | journal = Oncogene | volume = 8 | issue = 10 | pages = 2857–62 | date = Oct 1993 | pmid = 8397371 }}{{cite web | title = Entrez Gene: EPHB3 EPH receptor B3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2049}}
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
EPHB3 has been shown to interact with MLLT4{{cite journal | vauthors = Hock B, Böhme B, Karn T, Yamamoto T, Kaibuchi K, Holtrich U, Holland S, Pawson T, Rübsamen-Waigmann H, Strebhardt K | title = PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 95 | issue = 17 | pages = 9779–84 | date = Aug 1998 | pmid = 9707552 | pmc = 21413 | doi = 10.1073/pnas.95.17.9779 | bibcode = 1998PNAS...95.9779H | doi-access = free }} and RAS p21 protein activator 1.{{cite journal | vauthors = Hock B, Böhme B, Karn T, Feller S, Rübsamen-Waigmann H, Strebhardt K | title = Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions | journal = Oncogene | volume = 17 | issue = 2 | pages = 255–60 | date = Jul 1998 | pmid = 9674711 | doi = 10.1038/sj.onc.1201907 | doi-access = free }}
References
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Further reading
{{refbegin|35em}}
- {{cite journal | vauthors = Flanagan JG, Vanderhaeghen P | s2cid = 1278600 | title = The ephrins and Eph receptors in neural development. | journal = Annu. Rev. Neurosci. | volume = 21 | pages = 309–45 | year = 1998 | pmid = 9530499 | doi = 10.1146/annurev.neuro.21.1.309 | url = http://pdfs.semanticscholar.org/3025/541990c922c038dc20b0131fbd6e512e4c6d.pdf | archive-url = https://web.archive.org/web/20190221230330/http://pdfs.semanticscholar.org/3025/541990c922c038dc20b0131fbd6e512e4c6d.pdf | url-status = dead | archive-date = 2019-02-21 }}
- {{cite journal | vauthors = Zhou R | title = The Eph family receptors and ligands. | journal = Pharmacol. Ther. | volume = 77 | issue = 3 | pages = 151–81 | year = 1998 | pmid = 9576626 | doi = 10.1016/S0163-7258(97)00112-5 }}
- {{cite journal | vauthors = Holder N, Klein R | title = Eph receptors and ephrins: effectors of morphogenesis. | journal = Development | volume = 126 | issue = 10 | pages = 2033–44 | year = 1999 | doi = 10.1242/dev.126.10.2033 | pmid = 10207129 }}
- {{cite journal | vauthors = Wilkinson DG | title = Eph receptors and ephrins: regulators of guidance and assembly. | journal = Int. Rev. Cytol. | volume = 196 | pages = 177–244 | year = 2000 | pmid = 10730216 | doi = 10.1016/S0074-7696(00)96005-4 | series = International Review of Cytology | isbn = 9780123646002 }}
- {{cite journal | vauthors = Xu Q, Mellitzer G, Wilkinson DG | title = Roles of Eph receptors and ephrins in segmental patterning. | journal = Philos. Trans. R. Soc. Lond. B Biol. Sci. | volume = 355 | issue = 1399 | pages = 993–1002 | year = 2001 | pmid = 11128993 | pmc = 1692797 | doi = 10.1098/rstb.2000.0635 }}
- {{cite journal | vauthors = Wilkinson DG | title = Multiple roles of EPH receptors and ephrins in neural development. | journal = Nat. Rev. Neurosci. | volume = 2 | issue = 3 | pages = 155–64 | year = 2001 | pmid = 11256076 | doi = 10.1038/35058515 | s2cid = 205014301 }}
- {{cite journal | vauthors = Böhme B, VandenBos T, Cerretti DP, Park LS, Holtrich U, Rübsamen-Waigmann H, Strebhardt K | title = Cell-cell adhesion mediated by binding of membrane-anchored ligand LERK-2 to the EPH-related receptor human embryonal kinase 2 promotes tyrosine kinase activity. | journal = J. Biol. Chem. | volume = 271 | issue = 40 | pages = 24747–52 | year = 1996 | pmid = 8798744 | doi = 10.1074/jbc.271.40.24747 | doi-access = free }}
- {{cite journal | vauthors = Ephnomenclaturecommittee | title = Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee. | journal = Cell | volume = 90 | issue = 3 | pages = 403–4 | year = 1997 | pmid = 9267020 | doi = 10.1016/S0092-8674(00)80500-0 | s2cid = 26773768 | doi-access = free }}
- {{cite journal | vauthors = Bergemann AD, Zhang L, Chiang MK, Brambilla R, Klein R, Flanagan JG | title = Ephrin-B3, a ligand for the receptor EphB3, expressed at the midline of the developing neural tube. | journal = Oncogene | volume = 16 | issue = 4 | pages = 471–80 | year = 1998 | pmid = 9484836 | doi = 10.1038/sj.onc.1201557 | doi-access = free }}
- {{cite journal | vauthors = Hock B, Böhme B, Karn T, Feller S, Rübsamen-Waigmann H, Strebhardt K | title = Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions. | journal = Oncogene | volume = 17 | issue = 2 | pages = 255–60 | year = 1998 | pmid = 9674711 | doi = 10.1038/sj.onc.1201907 | doi-access = free }}
- {{cite journal | vauthors = Hock B, Böhme B, Karn T, Yamamoto T, Kaibuchi K, Holtrich U, Holland S, Pawson T, Rübsamen-Waigmann H, Strebhardt K | title = PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 95 | issue = 17 | pages = 9779–84 | year = 1998 | pmid = 9707552 | pmc = 21413 | doi = 10.1073/pnas.95.17.9779 | bibcode = 1998PNAS...95.9779H | doi-access = free }}
- {{cite journal | vauthors = Ciossek T, Monschau B, Kremoser C, Löschinger J, Lang S, Müller BK, Bonhoeffer F, Drescher U | title = Eph receptor-ligand interactions are necessary for guidance of retinal ganglion cell axons in vitro. | journal = Eur. J. Neurosci. | volume = 10 | issue = 5 | pages = 1574–80 | year = 1998 | pmid = 9751130 | doi = 10.1046/j.1460-9568.1998.00180.x | s2cid = 20470923 }}
- {{cite journal | vauthors = Adams RH, Wilkinson GA, Weiss C, Diella F, Gale NW, Deutsch U, Risau W, Klein R | title = Roles of ephrinB ligands and EphB receptors in cardiovascular development: demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis. | journal = Genes Dev. | volume = 13 | issue = 3 | pages = 295–306 | year = 1999 | pmid = 9990854 | pmc = 316426 | doi = 10.1101/gad.13.3.295 }}
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External links
- {{PDBe-KB2|P54753|Ephrin type-B receptor 3}}
{{Tyrosine kinases}}
{{Enzymes}}
{{Growth factor receptor modulators}}
{{Portal bar|Biology|border=no}}
Category:Tyrosine kinase receptors
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