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that expression of EFNB1 and EFNB2 (show EFNB2 Proteins) is implicated in Th cell differentiation and migration to inflammatory sites in both EAE and MS
germinal center (GC)-expressed ephrin B1 (EFNB1) repulsively inhibited T cell to B (show TDO2 Proteins) cell adhesion and GC follicular T helper retention by signaling through TFH-expressed EPHB6 (show EPHB6 Proteins) receptor; at the same time, EFNB1 promoted interleukin-21 (show IL21 Proteins) production from GC TFH cells by signaling predominantly through EPHB4 (show EPHB4 Proteins)
these observations demonstrate the importance of ephrinB1 signalling between cells of the skeleton required for endochondral ossification.
an autonomous receptor-like role for ephrin-B reverse signaling in the tangential migration of interneurons into the neocortex using ephrin-B (EfnB1/B2/B3) conditional triple mutant (TM(lz)) mice, is reported.
These results indicate a novel mechanism of ephrin-Eph (show EPHA1 Proteins) signaling independent of direct cell contact and proteolytic cleavage and suggest the participation of EphB2 (show EPHB2 Proteins)(+) extracellular vesicles in neural development and synapse physiology.
ephrin-B1-mediated cell segregation occurs in the early neuroepithelium.
Results suggest the involvement of ephrin-B1 signaling in astrocyte-mediated remodeling of excitatory synapses following injury, which can be accomplished through ephrin-B1-mediated regulation of STAT3 (show STAT3 Proteins) signaling in astrocytes.
Conditioned deletion of ephrinB1 and/or ephrinB2 (show EFNB2 Proteins) in either thymocytes or thymic epithelial cells alters the organization of thymic medulla and favors the appearance of thymic epithelial cysts.
Efnb1 and Efnb2 in T cells are essential for pathogenic antibody production and for T cell migration to the inflamed paws in mice with collagen-induced arthritis.
The EphB2 (show EPHB2 Proteins) and ephrin-B1 are possibly involved in epithelial boundary formation at the squamocolumnar junction.
bidirectional signaling between EphrinB1 and EphB3b coordinates the movements of the hepatic endoderm and adjacent lateral plate mesoderm (LPM), resulting in asymmetric positioning of the zebrafish liver.
we demonstrate that mosaicism for EPHRIN-B1 expression induced by random X inactivation in heterozygous females results in robust cell segregation in human neuroepithelial cells, thus supplying experimental evidence that Eph (show EPHA1 Proteins)/ephrin-mediated cell segregation is relevant to pathogenesis in human CFNS patients.
one novel (IVS2+3G>T) and one previously reported mutation (p.Gly151Ser) in EFNB1 Both patients were de novo cases without a family history of Craniofrontonasal syndrome.
While ephrin-B1 deficiency leads to abnormal visual pathways in mice, it leaves the human visual system, apart from deficits in binocular vision, largely normal.
that EphrinB1 (EFNB1) co-localizes with microtubules (MTs (show TIMM8A Proteins)) during all phases of the cell cycle.
we report a family with a G151S mutation in the EFNB1 gene. The mutation was identified in two severely affected sisters and paradoxically in their clinically unaffected father.
T cells from rheumatoid arthritis (RA) patients expressed higher EFNB1 mRNA levels, which correlated with RA symptoms and laboratory findings. Expression of EFNB1 in T cells might be a parameter for monitoring RA disease activity and treatment responses.
Results indicate that EphrinB1 is uniquely dysregulated in medulloblastoma and promotes oncogenic responses in medulloblastoma cells, implicating ephrinB1 as a potential target
EphB2 (show EPHB2 Proteins)/ephrin-B1 were invoked in dental pulp stem cells with TNF-alpha (show TNF Proteins) treatment via the JNK (show MAPK8 Proteins)-dependent pathway, but not NF-kB, p38 MAPK (show MAPK14 Proteins) or MEK (show MAP2K1 Proteins) signalling.
Patients with EFNB1 mutations have a clear phenotype. This study will facilitate genetic counseling of parents and patients, and contribute to the diagnostic and screening process of patients with suspected CFNS.
interactions between Smurfs and ephrinB1 regulates the maintenance of tissue boundaries through the control of ephrinB protein levels
Results identify the transcriptional co-repressor xTLE1/Groucho as an EphrinB1 interacting protein.
Ephrin-B1 and Wnt3A (show WNT3A Proteins) signaling contribute to region-specific neuronal plasticity in the developing optic tectum.
Tyrosine-298 in ephrin B1 is required for binding Grb4 (show NCK2 Proteins).
EphrinB1 reverse signaling is required to promote cellular movements into the eye field, and can rescue the FGF receptor (show FGFR2 Proteins)-induced repression of retinal fate. respectively.
Gain- and loss-of-function experiments suggest that Xdsh (show DVL2 Proteins) associates with ephrinB1 and mediates ephrinB1 signalling through downstream members of the PCP (show PRCP Proteins) pathway during eye field formation.
recruitment of STAT3 (show STAT3 Proteins) to ephrinB1, and its resulting Jak2 (show JAK2 Proteins)-dependent activation and transcription of reporter targets, reveals a signaling pathway from ephrinB1 to the nucle
ephrinB1 associates with the Par (show AFG3L2 Proteins) polarity complex protein Par-6 (show PARD6A Proteins) and can compete with the small GTPase (show RACGAP1 Proteins) Cdc42 (show CDC42 Proteins) for association with Par-6 (show PARD6B Proteins).
Data demonstrate that phosphorylation of tyrosines 324 and 325 of ephrin B1 disrupts the ephrinB1/Dishevelled (show DVL2 Proteins) interaction, thus modulating retinal progenitor movement that is dependent on the planar cell polarity pathway.
The protein encoded by this gene is a type I membrane protein and a ligand of Eph-related receptor tyrosine kinases. It may play a role in cell adhesion and function in the development or maintenance of the nervous system.
, EPH-related receptor tyrosine kinase ligand 2
, ELK ligand
, CEK5 receptor ligand
, Cek ligand
, Cek5 ligand
, stimulated by retinoic acid gene 1 protein
, eph-related receptor tyrosine kinase ligand 2
, ligand of eph-related kinase 2
, ephrin-B1 (EPH family ligand)
, CEK5 ligand