Ephrin type B-1 receptor is a protein encoded by a gene EPHB1 in humans. And its ligand ephrin receptor, ephrin, many processes of development of the nervous system in particular mediation,. Based on the sequence context and their structure, ephrins are divided into (EFNA) Class ephrin-A, which is fixed to the membrane by (EFNB) Class ephrin-B is a transmembrane protein and glycosylphosphatidylinositol linkage. Eph family of receptors are divided into two groups based on the similarity of their affinity for ephrin ligand binding and ephrin-AB extracellular domain sequence thereof. I comprises a subgroup of the maximum ephrin receptor tyrosine kinase (RTK) family. protein this gene encodes is a receptor that interacts with NCK1 B1 receptor of ephrin-B family members. EPH and GRB7, ACP1 is shown.

And its ligand ephrin receptor, ephrin, many processes of development of the nervous system in particular mediation,. Based on the sequence context and their structure, ephrins are divided into (EFNA) Class ephrin-A, which is fixed to the membrane by (EFNB) Class ephrin-B is a transmembrane protein and glycosylphosphatidylinositol linkage. Eph family of receptors are divided into two groups based on the similarity of their affinity for ephrin ligand binding and ephrin-AB extracellular domain sequence thereof. I comprises a subgroup of the maximum ephrin receptor tyrosine kinase (RTK) family. protein this gene encodes is a receptor of ephrin-B family members.

The Eph family of neural pathfinding directly the migration area of ​​cells (including the EphA3, EphB4) receptor tyrosine kinase expressing the slope of the membrane binding their ligands. Direct vascular network assembly (the EphA2 and EphB1) Other affect the angiogenic endothelial migration, and capillary morphogenesis. They in order to explore whether there can be provided a position label ephrin battery of target, we and P19 EphB1 (ELK) and form between endogenous endothelial cell oligomer another EPHB2 (SSC the ephrin-B1/Fc ligand synthesis I was tested receptor) whether discrimination. Dimers and receptor tyrosine phosphorylation, stimulate both the cluster a large amount ephrin-B1, but a large amount of body ephrin-B1 only (tetramer) to the receptor complex, low-molecular-weight phosphorylated tyrosine phosphatase (LMW- We are promoting endothelial capillary-like assembly of PTP), employment and cell adhesion. Must be EphB1 complex adoption and EphB1 activation of LMW-PTP is cell-to-cell contact between cells expressing ephrin-B1 and EphB1. Mapped as required for ephrin-B1 tetramer promote attachment recruitment and LMW-PTP, LMW-PTP for EphB1-binding site were shown. Thus, the key mechanism receptor EphB1, the ephrin-B1 oligomers various variety of cell signaling responses and various assembly complex is determined by the sensitive bond.

Based on these results, it is possible that this alternative indication reflects differential recruitment of signaling components of complexes with activated receptors by multimeric or ephrin-B1 dimer we I reasoned with. To examine this question, we analyzed the EphB1 complexes recovered after stimulation with a large amount ephrin-B1/Fc or dimer. NCK SH2-containing adapter protein, and GRB2, GRB10 was appointed EphB1 complex (not shown) with an efficiency that distinguish a large amount of body and ephrin-B1 dimer can not tell. But by EphB1 receptor EPHB2 phosphotyrosine immunity, and phosphorus selection of low-molecular-weight specific you are engaged after activation of ephrin-B1 abundance (18 KD),. Yeast two-hybrid screen of EphB1-Terra protein E9.5-E10.5 mouse library does not provide the candidate of 18 kD. A recent report, however, LMW-PTP itself human indicates that it is a substrate for tyrosine phosphorylation of V-Src. Therefore, EphB1 immunoprecipitation analysis of immunoreactivity of LMW-PTP we. Affinity-purified LMW-PTP antibody recognizes a 18-III tyrosine phosphorylation EPHB2 signaling complex and activation after a large amount of EphB1, but we found that it is not a ephrin-B1 dimer.

And its ligand ephrin receptor, ephrin, many processes of development of the nervous system in particular mediation,. On the basis of their sequence and structure relationship, ephrin is divided ephrin-A in (EFNA) class. They are fixed to the membrane by ephrin-B (EFNB) class and glycosyl bond is the transmembrane protein. Eph family of receptors are divided into two groups based on the similarity of their affinity for ephrin ligand binding and ephrin-AB extracellular domain sequence thereof. I comprises a subgroup of the maximum ephrin receptor tyrosine kinase (RTK) family. protein this gene encodes is a receptor of ephrin-B family members.

Receptor tyrosine kinase that binds to the ligand ephrin-B through a plurality of the contact-dependent bidirectional device adjacent cells, so that families present in the cells adjacent to each other. Downstream between signaling pathways ligand ephrin reverse signaling is called downstream signaling the first signaling path of the receptor. EFNB3 and EFNB1, EFNB2 relatives / ephrin ligand function is included for this receptor. During the development of the nervous system, to regulate axon guidance re the same side of the retina retina ventrotemporal  Axons of ganglion cells in the midline of the optic chiasm. This requires a repulsive interaction and EFNB2 probably. In the nervous system of adult EFNB3, chemotaxis, cell proliferation, and I adjust the polarity of hippocampal neural progenitor cells. In addition to its role in axon guidance, and plays an important role redundant with ephrin-B receptor of other mature development and synapse formation and dendritic spines. In addition, you may want to adjust the angiogenesis. In general, I may play an important role in the adhesion and migration of target cells more. To activate the ephrin-B ligand when the other or perhaps activation of EFNB1, respectively, JNK signaling cascade and MAPK / ERK regulates adhesion and cell migration

Four hetero ligand binding. I consists of ephrin receptor dimer and tetramer hetero. Oligomerization, it is necessary to induce a biological response probably. Interact with EPHB6, transphosphorylates the EPHB6 to form a signaling complex active. I interact with PICK1 (similar). I interact To be (via SH2 domain), a cascade of June that the activated, regulate cell adhesion and (C similarity) (-594 different tyrosine) NCK1. Ligand-activated form interacts (Tyr-928 via) to be (via SH2 domain) GRB10 and GRB7. (Via SH2 domain) ligand-activated form react (residues of the catalytic domain) of GRB2. Is reacted with SRC and GRB2, SHC1, and active MAPK / ERK cascade in regulation of cell migration. To regulate the degradation of the receptor by ubiquitination; interact with CBL. Interact with ACP1

EphB1 receptor tyrosine kinase family of Ephesus. And ephrin-B1, B2, B3: Members of the ephrin-B receptor family. Ephesians largest receptor tyrosine kinase family, in the tyrosine kinase group, has 14 members. They bind to the repulsive adhesion of cells to be place for membrane-anchored ligand, ephrin, of cell-cell contact, the establishment of a model of a mobile organization, the basis for the renovation and maintenance. EPH signal development, it is particularly important in the control of cell migration and cell adhesion of homeostasis and disease during axon guidance. EPHA receptors bind to ephrin ligands GPI anchor while bound to ephrin-B proteins with transmembrane and cytoplasmic domains are EPHB receptors. Interaction of ephrin-B proteins between the receptor kinase EPHB converts signaling cell types interaction both bidirectional signals. Adjust the adhesion of endothelial cells Eph receptors and ephrins and, it is necessary for the reconstruction of the vessel. Ligand activated form of EphB1 was reacted with NCK and GRB2, GRB10 through the SH2 domain of each. Four alternative splicing isoforms are known. Note: This description may include information from UniProtKB.