Ephrin B3: Difference between revisions

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| summary_text = EFNB3, a member of the [[ephrin]] gene family, is important in brain development as well as in its maintenance. The EPH and EPH-related receptors comprise the largest subfamily of [[receptor protein-tyrosine kinases]]. EPH receptors typically have a single [[kinase]] domain and an extracellular region containing a Cysteine-rich domain and 2 fibronectin type III repeats. The ephrin ligands and receptors have been named by the Eph Nomenclature Committee (1997) 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. Ephrin-B ligands also contain an intracellular tail with highly conserved [[tyrosine]] residues and a PDZ-binding motif at the [[C-terminus]].<ref name="Klein">{{cite journal|last=Klein|first=Rudiger|title=Eph/ephrin signalling during development|journal=Development|date=November 15, 2012|doi=10.1242/dev.074997|pmid=23093422|volume=139|issue=22|pages=4105–9}}</ref>  This tail functions as a mechanism for reverse signaling, where signaling occurs into the ligand-containing cell, as opposed to the cell with the receptor. Upon receptor-ligand interaction the tyrosine residues become phosphorylated and there is recruitment of [[PDZ domain]]-containing proteins.<ref name="Klein"/> The Eph family of receptors are similarly divided into two groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.<ref name="entrez"/>
| summary_text = EFNB3, a member of the [[ephrin]] gene family, is important in brain development as well as in its maintenance. The EPH and EPH-related receptors comprise the largest subfamily of [[receptor protein-tyrosine kinases]]. EPH receptors typically have a single [[kinase]] domain and an extracellular region containing a Cysteine-rich domain and 2 fibronectin type III repeats. The ephrin ligands and receptors have been named by the Eph Nomenclature Committee (1997) 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. Ephrin-B ligands also contain an intracellular tail with highly conserved [[tyrosine]] residues and a PDZ-binding motif at the [[C-terminus]].<ref name="Klein">{{cite journal|last=Klein|first=Rudiger|title=Eph/ephrin signalling during development|journal=Development|date=November 15, 2012|doi=10.1242/dev.074997|pmid=23093422|volume=139|issue=22|pages=4105–9}}</ref>  This tail functions as a mechanism for reverse signaling, where signaling occurs into the ligand-containing cell, as opposed to the cell with the receptor. Upon receptor-ligand interaction the tyrosine residues become phosphorylated and there is recruitment of [[PDZ domain]]-containing proteins.<ref name="Klein"/> The Eph family of receptors are similarly divided into two groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.<ref name="entrez"/>
}}
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EphrinB3 has been implicated in mediating various developmental events, particularly in the [[nervous system]]. EphrinB3 reverse signaling is important for axon pruning and synapse and spine formation during postnatal development of the nervous system.<ref name="Rodger 2012">{{cite journal|last=Rodger|first=Jennifer|author2=Lorena Salvatore |author3=Paolo Migani |title=Should I Stay or Should I Go? Ephs and Ephrins in Neuronal Migration|journal=Neurosignals|year=2012|doi=10.1159/000333784|pmid=22456188|volume=20|issue=3|pages=190–201}}</ref><ref name="Hruska 2012">{{cite journal|last=Hruska|first=Martin|author2=Matthew B. Dalva|title=Ephrin regulation of synapse formation, function and plasticity|journal=Molecular and Cellular Neuroscience|year=2012|doi=10.1016/j.mcn.2012.03.004|pmid=22449939|volume=50|issue=1|pages=35–44}}</ref>  Previous work has also shown that signaling through this ligand is important for radial migration during cortical development.<ref name="Rodger 2012"/> Moreover, levels of EFNB3 expression are particularly high in several [[forebrain]] subregions compared to other brain subregions, and may play a pivotal role in forebrain function. It has been suggested that ephrinB3 signaling is necessary for [[synaptic plasticity]] to occur in the [[hippocampus]]; this implicates ephrinB3 as a major player in learning and memory.<ref name="Hruska 2012"/> More recently, ephrinB3 has been shown to regulate proliferation of [[neural stem cell]]s in the adult [[subventricular zone]] (SVZ).<ref name="Rodger 2012"/><ref>{{cite journal|last=Ricard|first=Jerome|author2=Jessica Salinas |author3=Lissette Garcia |author4=Daniel J. Liebl |title=EphrinB3 regulates cell proliferation and survival in adult neurogenesis|journal=Molecular and Cellular Neuroscience|year=2006|doi=10.1016/j.mcn.2006.01.002|pmid=16483793 |volume=31 |issue=4 |pages=713–22}}</ref>
EphrinB3 has been implicated in mediating various developmental events, particularly in the [[nervous system]]. EphrinB3 reverse signaling is important for axon pruning and synapse and spine formation during postnatal development of the nervous system.<ref name="Rodger 2012">{{cite journal|last=Rodger|first=Jennifer|author2=Lorena Salvatore |author3=Paolo Migani |title=Should I Stay or Should I Go? Ephs and Ephrins in Neuronal Migration|journal=Neurosignals|year=2012|doi=10.1159/000333784|pmid=22456188|volume=20|issue=3|pages=190–201}}</ref><ref name="Hruska 2012">{{cite journal|last=Hruska|first=Martin|author2=Matthew B. Dalva|title=Ephrin regulation of synapse formation, function and plasticity|journal=Molecular and Cellular Neuroscience|year=2012|doi=10.1016/j.mcn.2012.03.004|pmid=22449939|volume=50|issue=1|pages=35–44|pmc=3631567}}</ref>  Previous work has also shown that signaling through this ligand is important for radial migration during cortical development.<ref name="Rodger 2012"/> Moreover, levels of EFNB3 expression are particularly high in several [[forebrain]] subregions compared to other brain subregions, and may play a pivotal role in forebrain function. It has been suggested that ephrinB3 signaling is necessary for [[synaptic plasticity]] to occur in the [[hippocampus]]; this implicates ephrinB3 as a major player in learning and memory.<ref name="Hruska 2012"/> More recently, ephrinB3 has been shown to regulate proliferation of [[neural stem cell]]s in the adult [[subventricular zone]] (SVZ).<ref name="Rodger 2012"/><ref>{{cite journal|last=Ricard|first=Jerome|author2=Jessica Salinas |author3=Lissette Garcia |author4=Daniel J. Liebl |title=EphrinB3 regulates cell proliferation and survival in adult neurogenesis|journal=Molecular and Cellular Neuroscience|year=2006|doi=10.1016/j.mcn.2006.01.002|pmid=16483793 |volume=31 |issue=4 |pages=713–22}}</ref>


==References==
==References==

Latest revision as of 16:28, 15 May 2018

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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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View/Edit Human

Ephrin-B3 is a protein that in humans is encoded by the EFNB3 gene.[1][2]

EFNB3, a member of the ephrin gene family, is important in brain development as well as in its maintenance. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases. EPH receptors typically have a single kinase domain and an extracellular region containing a Cysteine-rich domain and 2 fibronectin type III repeats. The ephrin ligands and receptors have been named by the Eph Nomenclature Committee (1997) 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. Ephrin-B ligands also contain an intracellular tail with highly conserved tyrosine residues and a PDZ-binding motif at the C-terminus.[3] This tail functions as a mechanism for reverse signaling, where signaling occurs into the ligand-containing cell, as opposed to the cell with the receptor. Upon receptor-ligand interaction the tyrosine residues become phosphorylated and there is recruitment of PDZ domain-containing proteins.[3] The Eph family of receptors are similarly divided into two groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.[2] EphrinB3 has been implicated in mediating various developmental events, particularly in the nervous system. EphrinB3 reverse signaling is important for axon pruning and synapse and spine formation during postnatal development of the nervous system.[4][5] Previous work has also shown that signaling through this ligand is important for radial migration during cortical development.[4] Moreover, levels of EFNB3 expression are particularly high in several forebrain subregions compared to other brain subregions, and may play a pivotal role in forebrain function. It has been suggested that ephrinB3 signaling is necessary for synaptic plasticity to occur in the hippocampus; this implicates ephrinB3 as a major player in learning and memory.[5] More recently, ephrinB3 has been shown to regulate proliferation of neural stem cells in the adult subventricular zone (SVZ).[4][6]

References

  1. ↑ Tang XX, Pleasure DE, Ikegaki N (May 1997). "cDNA cloning, chromosomal localization, and expression pattern of EPLG8, a new member of the EPLG gene family encoding ligands of EPH-related protein-tyrosine kinase receptors". Genomics. 41 (1): 17–24. doi:10.1006/geno.1997.4615. PMID 9126477.
  2. ↑ 2.0 2.1 "Entrez Gene: EFNB3 ephrin-B3".
  3. ↑ 3.0 3.1 Klein, Rudiger (November 15, 2012). "Eph/ephrin signalling during development". Development. 139 (22): 4105–9. doi:10.1242/dev.074997. PMID 23093422.
  4. ↑ 4.0 4.1 4.2 Rodger, Jennifer; Lorena Salvatore; Paolo Migani (2012). "Should I Stay or Should I Go? Ephs and Ephrins in Neuronal Migration". Neurosignals. 20 (3): 190–201. doi:10.1159/000333784. PMID 22456188.
  5. ↑ 5.0 5.1 Hruska, Martin; Matthew B. Dalva (2012). "Ephrin regulation of synapse formation, function and plasticity". Molecular and Cellular Neuroscience. 50 (1): 35–44. doi:10.1016/j.mcn.2012.03.004. PMC 3631567. PMID 22449939.
  6. ↑ Ricard, Jerome; Jessica Salinas; Lissette Garcia; Daniel J. Liebl (2006). "EphrinB3 regulates cell proliferation and survival in adult neurogenesis". Molecular and Cellular Neuroscience. 31 (4): 713–22. doi:10.1016/j.mcn.2006.01.002. PMID 16483793.

Further reading



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