integral component of postsynaptic density membrane
Biological process
ephrin receptor signaling pathway
multicellular organism development
cell-cell signaling
viral entry into host cell
T cell costimulation
cell differentiation
viral process
axon choice point recognition
nervous system development
adult walking behavior
axon guidance
peptidyl-tyrosine phosphorylation
negative regulation of axonogenesis
trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
1949
13643
Ensembl
ENSG00000108947
ENSMUSG00000003934
UniProt
Q15768
O35393
RefSeq (mRNA)
NM_001406
NM_007911
RefSeq (protein)
NP_001397
NP_031937
Location (UCSC)
Chr 17: 7.71 – 7.71 Mb
Chr 11: 69.44 – 69.45 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Ephrin-B3 is a protein that in humans is encoded by the EFNB3 gene.[5][6]
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.[7] 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.[7] 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.[6]
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.[8][9] Previous work has also shown that signaling through this ligand is important for radial migration during cortical development.[8] 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.[9] More recently, ephrinB3 has been shown to regulate proliferation of neural stem cells in the adult subventricular zone (SVZ).[8][10]
^ abcGRCh38: Ensembl release 89: ENSG00000108947 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000003934 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^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.
^ abcRodger, 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.
^ abHruska, 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.
^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. S2CID 206830930.
Ephrin-B3 is a protein that in humans is encoded by the EFNB3 gene. EFNB3, a member of the ephrin gene family, is important in brain development as well...
shown that ephrin-B3 is able to bind to and activate EPH receptor A4 and ephrin-A5 can bind to and activate Eph receptor B2. EphAs/ephrin-As typically...
recently been shown that ephrin-B3 can bind to and activate EphA4 and that ephrin-A5 can bind to and activate EphB2. EphA/ephrinA interaction typically...
target cells that results in tyrosine phosphorylation of ephrin-B3. Ensuing binding of ephrin-B3 to the cytoplasmic adaptor protein, Grb4, leads to the...
their PDZ domains to stabilize newly formed CNS synapses. For example, EphrinB3 interacts with the adaptor protein glutamate-receptor-interacting protein...
immunization using a human monoclonal antibody, m102.4, that targets the ephrin-B2 and ephrin-B3 receptor-binding domain of the henipavirus Nipah G glycoprotein...
NgR1, p75, TROY and LINGO1. OMgp –Oligodendrocyte myelin glycoprotein EphrinB3 functions through the EphA4 receptor and inhibits remyelination. Sema...
EPH receptor A4 (ephrin type-A receptor 4) is a protein that in humans is encoded by the EPHA4 gene. This gene belongs to the ephrin receptor subfamily...
Ephrin B1 is a protein that in humans is encoded by the EFNB1 gene. It is a member of the ephrin family. The encoded protein is a type I membrane protein...
Ephrin type-B receptor 3 is a protein that in humans is encoded by the EPHB3 gene. Ephrin receptors and their ligands, the ephrins, mediate numerous developmental...
Ephrin-B2 is a protein that in humans is encoded by the EFNB2 gene. This gene encodes a member of the ephrin (EPH) family. The ephrins and EPH-related...
Ephrin A5 is a protein that in humans is encoded by the EFNA5 gene. Ephrin A5 is a glycosylphosphatidylinositol (GPI)-anchored protein of the ephrin-A...
Ephrin A1 is a protein that in humans is encoded by the EFNA1 gene. This gene encodes a member of the ephrin (EPH) family. The ephrins and EPH-related...
Ephrin-A2 is a protein that in humans is encoded by the EFNA2 gene. This gene encodes a member of the ephrin family. The protein is composed of a signal...
studies. Unlike Hendra and Nipah, which attach to Ephrin B2 or B3, Cedar virus can also attach to Ephrin B1. This may be responsible for lack of observed...
Ephrin type-B receptor 4 is a protein that in humans is encoded by the EPHB4 gene. Ephrin receptors and their ligands, the ephrins, mediate numerous developmental...
Ephrin A4 is a protein that in humans is encoded by the EFNA4 gene. This gene encodes a member of the ephrin (EPH) family. The ephrins and EPH-related...
Ephrin A3 is a protein that in humans is encoded by the EFNA3 gene. This gene encodes a member of the ephrin (EPH) family. The ephrins and EPH-related...
which mediates membrane fusion. Ephrins B2 and B3 have been identified as the main receptors for Nipah virus. Ephrin sub-types have a complex distribution...
Broder, Christopher C.; Nikolov, Dimitar B. (February 2012). "Ephrin-B2 and ephrin-B3 as functional henipavirus receptors". Seminars in Cell & Developmental...
Autophagy related 13 (KIAA0652), RB1-inducible coiled-coil 1 (RB1CC1), and Ephrin-B3 (EFNB3) . These proteins are predicted to be localized in the nucleus...
gene. ErbB3 is a member of the epidermal growth factor receptor (EGFR/ERBB) family of receptor tyrosine kinases. The kinase-impaired ErbB3 is known to...
PMID 21494248. Pascall JC, Brown KD (April 2004). "Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2". Biochemical and Biophysical...
MojV-G) is to attach the virus to the surface of a host cell via Ephrin B1, B2, or B3, a family of highly conserved mammalian proteins. The structure of...