View source for Ephrin B2

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{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
'''Ephrin-B2''' is a [[protein]] that in humans is encoded by the ''EFNB2'' [[gene]].<ref name="pmid7833926">{{cite journal | vauthors = Bonaldo MF, Yu MT, Jelenc P, Brown S, Su L, Lawton L, Deaven L, Efstratiadis A, Warburton D, Soares MB | title = Selection of cDNAs using chromosome-specific genomic clones: application to human chromosome 13 | journal = Human Molecular Genetics | volume = 3 | issue = 9 | pages = 1663–73 | date = Sep 1994 | pmid = 7833926 | doi = 10.1093/hmg/3.9.1663 }}</ref>
== Function ==
This gene encodes a member of the [[ephrin]] (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in [[erythropoiesis]]. 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. This gene encodes an EFNB class ephrin which binds to the [[EPHB4]] and [[EPHA3]] receptors.<ref name="entrez">{{cite web | title = Entrez Gene: EFNB2 ephrin-B2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1948}}</ref>
== Cancer ==
EFNB2 gene has been observed progressively downregulated in [[Human papillomavirus]]-positive [[Neoplasm|neoplastic keratinocytes]] derived from uterine cervical [[Cervical intraepithelial neoplasia|preneoplastic lesions]] at different levels of malignancy.<ref name = "Rotondo_2015">{{cite journal | vauthors = Rotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R, Torresani S, Marci R, Garutti P, Negrini M, Tognon M, Martini F | title = Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes. | journal = J Cell Physiol | volume = 230| issue = 4 | pages = 802–812 | date = April 2015 | pmid = 25205602 | doi = 10.1002/jcp.24808 | hdl = 11392/2066612 | s2cid = 24986454 | hdl-access = free }}</ref> For this reason, EFNB2 is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical [[Cervical intraepithelial neoplasia|preneoplastic lesions]] progression.<ref name="Rotondo_2015"/>
== Interactions ==
EFNB2 has been shown to [[Protein-protein interaction|interact]] with [[EPHA3]]<ref name=pmid8559144>{{cite journal | vauthors = Cerretti DP, Vanden Bos T, Nelson N, Kozlosky CJ, Reddy P, Maraskovsky E, Park LS, Lyman SD, Copeland NG, Gilbert DJ | title = Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases | journal = Molecular Immunology | volume = 32 | issue = 16 | pages = 1197–205 | date = Nov 1995 | pmid = 8559144 | doi = 10.1016/0161-5890(95)00108-5 | url = https://zenodo.org/record/1258339 }}</ref><ref name=pmid9195962>{{cite journal | vauthors = Lackmann M, Mann RJ, Kravets L, Smith FM, Bucci TA, Maxwell KF, Howlett GJ, Olsson JE, Vanden Bos T, Cerretti DP, Boyd AW | title = Ligand for EPH-related kinase (LERK) 7 is the preferred high affinity ligand for the HEK receptor | journal = The Journal of Biological Chemistry | volume = 272 | issue = 26 | pages = 16521–30 | date = Jun 1997 | pmid = 9195962 | doi = 10.1074/jbc.272.26.16521 | doi-access = free }}</ref> and [[EPHB1]] in [[optic chiasm]] development.<ref>{{cite journal | vauthors = Williams SE, Mann F, Erskine L, Sakurai T, Wei S, Rossi DJ, Gale NW, Holt CE, Mason CA, Henkemeyer M | title = Ephrin-B2 and EphB1 mediate retinal axon divergence at the optic chiasm | journal = Neuron | volume = 39 | issue = 6 | pages = 919–35 | date = September 2003 | pmid = 12971893 | doi =  10.1016/j.neuron.2003.08.017| doi-access = free }}</ref>
EFNB2 has also been shown to serve as a receptor for [[Henipavirus|Hendra Virus and Nipah Virus]], mediating [[Viral entry|entry]] into the cell during infection.<ref>{{cite journal | vauthors = Bonaparte MI, Dimitrov AS, Bossart KN, Crameri G, Mungall BA, Bishop KA, Choudhry V, Dimitrov DS, Wang LF, Eaton BT, Broder CC | title = Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 102 | issue = 30 | pages = 10652–7 | date = July 2005 | pmid = 15998730 | doi = 10.1073/pnas.0504887102 | pmc = 1169237 | bibcode = 2005PNAS..10210652B | doi-access = free }}</ref>
== References ==
{{reflist}}
== Further reading ==
{{refbegin | 2}}
* {{cite journal | vauthors = Flanagan JG, Vanderhaeghen P | title = The ephrins and Eph receptors in neural development | journal = Annual Review of Neuroscience | volume = 21 | pages = 309–45 | year = 1998 | pmid = 9530499 | doi = 10.1146/annurev.neuro.21.1.309 }}
* {{cite journal | vauthors = Zhou R | title = The Eph family receptors and ligands | journal = Pharmacology & Therapeutics | volume = 77 | issue = 3 | pages = 151–81 | date = Mar 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 | date = May 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 = International Review of Cytology | volume = 196 | pages = 177–244 | year = 2000 | pmid = 10730216 | doi = 10.1016/S0074-7696(00)96005-4 | isbn = 9780123646002 }}
* {{cite journal | vauthors = Xu Q, Mellitzer G, Wilkinson DG | title = Roles of Eph receptors and ephrins in segmental patterning | journal = Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences | volume = 355 | issue = 1399 | pages = 993–1002 | date = Jul 2000 | 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 = Nature Reviews. Neuroscience | volume = 2 | issue = 3 | pages = 155–64 | date = Mar 2001 | pmid = 11256076 | doi = 10.1038/35058515 | s2cid = 205014301 }}
* {{cite journal | vauthors = Bennett BD, Zeigler FC, Gu Q, Fendly B, Goddard AD, Gillett N, Matthews W | title = Molecular cloning of a ligand for the EPH-related receptor protein-tyrosine kinase Htk | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 92 | issue = 6 | pages = 1866–70 | date = Mar 1995 | pmid = 7534404 | pmc = 42383 | doi = 10.1073/pnas.92.6.1866 | bibcode = 1995PNAS...92.1866B | doi-access = free }}
* {{cite journal | vauthors = Cerretti DP, Vanden Bos T, Nelson N, Kozlosky CJ, Reddy P, Maraskovsky E, Park LS, Lyman SD, Copeland NG, Gilbert DJ | title = Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases | journal = Molecular Immunology | volume = 32 | issue = 16 | pages = 1197–205 | date = Nov 1995 | pmid = 8559144 | doi = 10.1016/0161-5890(95)00108-5 | url = https://zenodo.org/record/1258339 }}
* {{cite journal | vauthors = Cerretti DP, Lyman SD, Kozlosky CJ, Copeland NG, Gilbert DJ, Jenkins NA, Valentine V, Kirstein MN, Shapiro DN, Morris SW | title = The genes encoding the eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3 | journal = Genomics | volume = 33 | issue = 2 | pages = 277–82 | date = Apr 1996 | pmid = 8660976 | doi = 10.1006/geno.1996.0192 | url = https://zenodo.org/record/1229677 }}
* {{cite journal | vauthors = Gale NW, Holland SJ, Valenzuela DM, Flenniken A, Pan L, Ryan TE, Henkemeyer M, Strebhardt K, Hirai H, Wilkinson DG, Pawson T, Davis S, Yancopoulos GD | title = Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis | journal = Neuron | volume = 17 | issue = 1 | pages = 9–19 | date = Jul 1996 | pmid = 8755474 | doi = 10.1016/S0896-6273(00)80276-7 | doi-access = free }}
* {{cite journal | vauthors = Holland SJ, Gale NW, Mbamalu G, Yancopoulos GD, Henkemeyer M, Pawson T | title = Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands | journal = Nature | volume = 383 | issue = 6602 | pages = 722–5 | date = Oct 1996 | pmid = 8878483 | doi = 10.1038/383722a0 | bibcode = 1996Natur.383..722H | hdl = 1807/9444 | s2cid = 4349898 | hdl-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 | date = Aug 1997 | pmid = 9267020 | doi = 10.1016/S0092-8674(00)80500-0 | doi-access = free }}
* {{cite journal | vauthors = Vogt T, Stolz W, Welsh J, Jung B, Kerbel RS, Kobayashi H, Landthaler M, McClelland M | title = Overexpression of Lerk-5/Eplg5 messenger RNA: a novel marker for increased tumorigenicity and metastatic potential in human malignant melanomas | journal = Clinical Cancer Research | volume = 4 | issue = 3 | pages = 791–7 | date = Mar 1998 | pmid = 9533549 }}
* {{cite journal | vauthors = Wang HU, Chen ZF, Anderson DJ | title = Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4 | journal = Cell | volume = 93 | issue = 5 | pages = 741–53 | date = May 1998 | pmid = 9630219 | doi = 10.1016/S0092-8674(00)81436-1 | doi-access = free }}
* {{cite journal | vauthors = Nikolova Z, Djonov V, Zuercher G, Andres AC, Ziemiecki A | title = Cell-type specific and estrogen dependent expression of the receptor tyrosine kinase EphB4 and its ligand ephrin-B2 during mammary gland morphogenesis | journal = Journal of Cell Science | volume = 111 | issue = 18 | pages = 2741–51 | date = Sep 1998 | doi = 10.1242/jcs.111.18.2741 | pmid = 9718367 }}
* {{cite journal | vauthors = Torres R, Firestein BL, Dong H, Staudinger J, Olson EN, Huganir RL, Bredt DS, Gale NW, Yancopoulos GD | title = PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands | journal = Neuron | volume = 21 | issue = 6 | pages = 1453–63 | date = Dec 1998 | pmid = 9883737 | doi = 10.1016/S0896-6273(00)80663-7 | doi-access = free }}
* {{cite journal | vauthors = Lin D, Gish GD, Songyang Z, Pawson T | title = The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif | journal = The Journal of Biological Chemistry | volume = 274 | issue = 6 | pages = 3726–33 | date = Feb 1999 | pmid = 9920925 | doi = 10.1074/jbc.274.6.3726 | doi-access = free }}
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{{PDB Gallery|geneid=1948}}
{{Intercellular signaling peptides and proteins}}
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