Biology:Ephrin B2
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Ephrin-B2 is a protein that in humans is encoded by the EFNB2 gene.[1]
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.[2]
Cancer
EFNB2 gene has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy.[3] For this reason, EFNB2 is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression.[3]
Interactions
EFNB2 has been shown to interact with EPHA3[4][5] and EPHB1 in optic chiasm development.[6]
EFNB2 has also been shown to serve as a receptor for Hendra Virus and Nipah Virus, mediating entry into the cell during infection.[7]
References
- ↑ "Selection of cDNAs using chromosome-specific genomic clones: application to human chromosome 13". Human Molecular Genetics 3 (9): 1663–73. Sep 1994. doi:10.1093/hmg/3.9.1663. PMID 7833926.
- ↑ "Entrez Gene: EFNB2 ephrin-B2". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=1948.
- ↑ 3.0 3.1 "Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes.". J Cell Physiol 230 (4): 802–812. April 2015. doi:10.1002/jcp.24808. PMID 25205602.
- ↑ "Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases". Molecular Immunology 32 (16): 1197–205. Nov 1995. doi:10.1016/0161-5890(95)00108-5. PMID 8559144. https://zenodo.org/record/1258339.
- ↑ "Ligand for EPH-related kinase (LERK) 7 is the preferred high affinity ligand for the HEK receptor". The Journal of Biological Chemistry 272 (26): 16521–30. Jun 1997. doi:10.1074/jbc.272.26.16521. PMID 9195962.
- ↑ "Ephrin-B2 and EphB1 mediate retinal axon divergence at the optic chiasm". Neuron 39 (6): 919–35. September 2003. doi:10.1016/j.neuron.2003.08.017. PMID 12971893.
- ↑ "Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus". Proceedings of the National Academy of Sciences of the United States of America 102 (30): 10652–7. July 2005. doi:10.1073/pnas.0504887102. PMID 15998730. Bibcode: 2005PNAS..10210652B.
Further reading
- "The ephrins and Eph receptors in neural development". Annual Review of Neuroscience 21: 309–45. 1998. doi:10.1146/annurev.neuro.21.1.309. PMID 9530499.
- "The Eph family receptors and ligands". Pharmacology & Therapeutics 77 (3): 151–81. Mar 1998. doi:10.1016/S0163-7258(97)00112-5. PMID 9576626.
- "Eph receptors and ephrins: effectors of morphogenesis". Development 126 (10): 2033–44. May 1999. doi:10.1242/dev.126.10.2033. PMID 10207129.
- "Eph receptors and ephrins: regulators of guidance and assembly". 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". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences 355 (1399): 993–1002. Jul 2000. doi:10.1098/rstb.2000.0635. PMID 11128993.
- "Multiple roles of EPH receptors and ephrins in neural development". Nature Reviews. Neuroscience 2 (3): 155–64. Mar 2001. doi:10.1038/35058515. PMID 11256076.
- "Molecular cloning of a ligand for the EPH-related receptor protein-tyrosine kinase Htk". Proceedings of the National Academy of Sciences of the United States of America 92 (6): 1866–70. Mar 1995. doi:10.1073/pnas.92.6.1866. PMID 7534404. Bibcode: 1995PNAS...92.1866B.
- "Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases". Molecular Immunology 32 (16): 1197–205. Nov 1995. doi:10.1016/0161-5890(95)00108-5. PMID 8559144. https://zenodo.org/record/1258339.
- "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". Genomics 33 (2): 277–82. Apr 1996. doi:10.1006/geno.1996.0192. PMID 8660976. https://zenodo.org/record/1229677.
- "Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis". Neuron 17 (1): 9–19. Jul 1996. doi:10.1016/S0896-6273(00)80276-7. PMID 8755474.
- "Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands". Nature 383 (6602): 722–5. Oct 1996. doi:10.1038/383722a0. PMID 8878483. Bibcode: 1996Natur.383..722H.
- "Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee". Cell 90 (3): 403–4. Aug 1997. doi:10.1016/S0092-8674(00)80500-0. PMID 9267020.
- "Overexpression of Lerk-5/Eplg5 messenger RNA: a novel marker for increased tumorigenicity and metastatic potential in human malignant melanomas". Clinical Cancer Research 4 (3): 791–7. Mar 1998. PMID 9533549.
- "Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4". Cell 93 (5): 741–53. May 1998. doi:10.1016/S0092-8674(00)81436-1. PMID 9630219.
- "Cell-type specific and estrogen dependent expression of the receptor tyrosine kinase EphB4 and its ligand ephrin-B2 during mammary gland morphogenesis". Journal of Cell Science 111 (18): 2741–51. Sep 1998. doi:10.1242/jcs.111.18.2741. PMID 9718367.
- "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands". Neuron 21 (6): 1453–63. Dec 1998. doi:10.1016/S0896-6273(00)80663-7. PMID 9883737.
- "The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif". The Journal of Biological Chemistry 274 (6): 3726–33. Feb 1999. doi:10.1074/jbc.274.6.3726. PMID 9920925.
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