CDB15:0000509 EFNB1 — EPHB1
Experimentally validated in Human, Mixed species; Orthology-inferred in Human, Mouse, Rat, Frog, Zebrafish, Chicken, Macaque, Pig, Dog, Cow, Chimp, Horse, Sheep
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Abstract
EphB1 associates with Grb7 and regulates cell migration.
The Journal of biological chemistry, 2002; PubMed, Homo sapiens EFNB1 — Homo sapiens EPHB1
ABSTRACT: EphB1 is a member of the Eph family of receptor tyrosine kinases that play important roles in diverse biological processes including nervous system development, angiogenesis, and neural synapsis formation and maturation. Grb7 is an adaptor molecule implicated in the regulation of cell migration. Here we report identification of an interaction between Grb7 and the cytoplasmic domain of EphB1 by using Grb7 as a "bait" in a yeast two-hybrid screening. Co-immunoprecipitation was used to confirm the interaction of Grb7 with the cytoplasmic domain of EphB1 as well as the full-length receptor in intact cells. This interaction is mediated by the SH2 domain of Grb7 and requires tyrosine autophosphorylation of EphB1. Furthermore, Tyr-928 of EphB1 was identified as the primary binding site for Grb7. Stimulation of endogenous EphB1 in embryonal carcinoma P19 cells with its ligand ephrinB1 increased its association with Grb7, which is consistent with a role for the autophosphorylation of EphB1. We also found that EphB1 could phosphorylate Grb7 and mutation of either Tyr-928 or Tyr-594 to Phe decreased this activity. Finally, we show that EphB1 could stimulate fibroblast motility on extracellular matrix in a kinase-dependent manner, which also correlated with its association with Grb7. Consistent with this, co-expression of Grb7 with EphB1 further enhanced cell motility, whereas co-expression of the Grb7 SH2 domain abolished EphB1-stimulated cell migration. Together, our results identified a novel interaction between EphB1 with the adaptor molecule Grb7 and suggested that this interaction may play a role in the regulation of cell migration by EphB1.
Characterization of a novel Eph receptor tyrosine kinase, EphA10, expressed in testis.
Biochimica et biophysica acta, 2005; PubMed, Homo sapiens EFNB1 — Homo sapiens EPHB1
ABSTRACT: In mammals, 14 members of the Eph receptor tyrosine kinase family have been described so far. Here we present a not yet described member of this family denoted EphA10. We report the identification of three putative EphA10 isoforms: one soluble and two transmembrane isoforms. One of the latter isoforms lacked the sterile alpha motif commonly found in Eph receptors. The gene encoding EphA10 is located on chromosome 1p34 and expression studies show that EphA10 mRNA is mainly expressed in testis. Binding studies to ephrin ligands suggests that this receptor belongs to the EphA subclass of Eph receptors binding mainly to ephrin-A ligands.
Profiling Eph receptor expression in cells and tissues: a targeted mass spectrometry approach.
Cell adhesion & migration, 2012; PubMed, Mus Musculus Efnb1 — Rattus norvegicus Ephb1
ABSTRACT: The Eph receptor tyrosine kinase family includes many members, which are often expressed together in various combinations and can promiscuously interact with multiple ephrin ligands, generating intricate networks of intracellular signals that control physiological and pathological processes. Knowing the entire repertoire of Eph receptors and ephrins expressed in a biological sample is important when studying their biological roles. Moreover, given the correlation between Eph receptor/ephrin expression and cancer pathogenesis, their expression patterns could serve important diagnostic and prognostic purposes. However, profiling Eph receptor and ephrin expression has been challenging. Here we describe a novel and straightforward approach to catalog the Eph receptors present in cultured cells and tissues. By measuring the binding of ephrin Fc fusion proteins to Eph receptors in ELISA and pull-down assays, we determined that a mixture of four ephrins is suitable for isolating both EphA and EphB receptors in a single pull-down. We then used mass spectrometry to identify the Eph receptors present in the pull-downs and estimate their relative levels. This approach was validated in cultured human cancer cell lines, human tumor xenograft tissue grown in mice, and mouse brain tissue. The new mass spectrometry approach we have developed represents a useful tool for the identification of the spectrum of Eph receptors present in a biological sample and could also be extended to profiling ephrin expression.