Ephrin type-B receptor 2 is a protein encoded by a gene in human EPHB2. 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. It comprises a subgroup of the maximum ephrin receptor tyrosine kinase (RTK) family. protein this gene encodes is a receptor of ephrin-B family members.


Effects related receptor tyrosine kinases are involved in the control of the navigation and fasciculation of axons. To investigate the biochemical mechanisms underlying these features, we NG108-15 neuronal cells EPHB2 receptor tyrosine phosphorylation of cellular proteins many of were observed during startup of the EPHB2 ligand ephrin-B1 (formerly Nuk/Cek5/Sek3) expression (formerly Elk-L/Lerk2). Activation EPHB2 receptor induces tyrosine phosphorylation of (P62 [DOK]) of 62-64 kDa protein forms a complex with the SH2/SH3 NCK adapter protein domain GTP GTPase-activating protein of Ras and (RasGAP) in order to. Bind via its SH2 domain tyrosine phosphorylation EPHB2 in in vitro, RasGAP is complexed with activated EPHB2 in vivo. Substitution of these amino acids I to show that you remove the ephrin-B1-induced signaling events in NG108-15 cells EPHB2 expression and Y610, and Y604 in the tyrosine residues juxtamembrane region EPHB2 saved localization vitro RasGAP binding site of the multi-level. Depending on the specificity of the binding of the SH2 domain determined by the RasGAP phosphopeptide libraries degeneration, 3 – and a tyrosine residue of these proline, followed by position. These results, identify the EPHB2 activation signaling cascade, including the proteins that play a role in the control and axon guidance of the cytoskeleton architecture potentially.


You can determine amyloid β oligomers whether directly interact with EPHB2, was measuring the binding of β1-42 oligomer purified biotinylated synthetic amyloid of chimera EPHB2-Fc recombinant. Pull-down avidin agarose beads EPHB2-FC and amyloid β oligomers biotinylated, cell cooperation immunoprecipitation with no conditions. From the homogenate (Supplementary Figure 2E-G) Co-immunoprecipitation primary neurons and amyloid β oligomers and EPHB2. Therefore, amyloid-β oligomers will be able to interact directly with the extracellular region of EPHB2.

This region includes (FN) fibronectin type III domain repeats ligand binding (LB) domain, cysteine-rich (CR) and domain. In order to measure the interaction with any domain-mediated amyloid β oligomers, we generated a deletion mutant of EPHB2-GST lacks the domain or FN (DLB-EPHB2) LB domain. I show that DFN-EPHB2, FN domain is important for interaction with EPHB2 but DLB-EPHB2 and amyloid β oligomers related-EPHB2 FL.

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. Function of axon guidance during development. I have participated in the management of the commissural axon is a connection of the main interhemispheric between two time units of the cerebral cortex.

We also participated in the axons of retinal ganglion cells of the optic nerve head and guidance of the inner ear opposite centrifugal growth cone of the center line. In addition, to adjust the development and maturation of dendritic spines, axon guidance also stimulate the formation of excitatory synapses. When activated the EFNB1, you can remove the adjustment of ARHGEF15 mediated negative in the formation of excitatory synapses. To control other aspects of development, such as inner ear development by regulating the production of endolymph and development angiogenesis, the palate. I regulate the adhesion and flow of block sewer tubularize cells and reverse urethra signaling through the complex EFNB2/EPHB2 and forward. It can function as a tumor suppressor

Four hetero ligand binding. I consists of ephrin receptor dimer and tetramer hetero. Oligomerization, it is necessary to induce a biological response probably. I will interact with PICK1 and GRIP1. ARHGEF15 mediated phosphorylation, ubiquitination and degradation by the proteasome; dialogue with ARHGEF15. Involved in the production of endolymph in the inner ear; dialogue with AQP1.

Amyloid-β oligomers, by inhibiting the NMDA glutamate receptor neurons whose function is regulated by the receptor tyrosine kinases EPHB2, may cause cognitive impairment in Alzheimer’s disease. In this case, the amyloid β oligomers shows a binding domain in the fibronectin repeat of EPHB2 degradation and trigger EPHB2 in the proteasome. To determine the importance of literature and depletion of EPHB2 Alzheimer influenza, we use the structure of the lentivirus to increase or decrease the expression of neurons EPHB2 memory center of the brain of the mouse was. The knockdown transgenic mice, of EPHB2, short RNA can mediate the impairment of long-term potentiation dentate gyrus and acute decompression NMDA receptor current important for memory formation. Mouse of the human amyloid precursor protein transgenic reverse defect in memory impairment and EPHB2, NMDA receptor-dependent long-term potentiation expression in the dentate gyrus was increased. Therefore, reduction of EPHB2 is important in amyloid-β-induced neuronal dysfunction. Or function EPHB2 level increased, I may be useful in the treatment of Alzheimer’s disease.