EPHB1

Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. 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. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by this gene is a receptor for ephrin-B family members. [provided by RefSeq, Jul 2008]

EPH Receptor B1

Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Cognate/functional ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During nervous system development, regulates retinal axon guidance redirecting ipsilaterally ventrotemporal retinal ganglion cells axons at the optic chiasm midline. This probably requires repulsive interaction with EFNB2. In the adult nervous system together with EFNB3, regulates chemotaxis, proliferation and polarity of the hippocampus neural progenitors. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. May also regulate angiogenesis. More generally, may play a role in targeted cell migration and adhesion. Upon activation by EFNB1 and probably other ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively. Involved in the maintenance of the pool of satellite cells (muscle stem cells) by promoting their self-renewal and reducing their activation and differentiation (By similarity).

Angiogenesis Source: UniProtKB
Axon guidance Source: UniProtKB
Camera-type eye morphogenesis Source: Ensembl
Cell chemotaxis Source: UniProtKB
Cell-substrate adhesion Source: UniProtKB
Central nervous system projection neuron axonogenesis Source: UniProtKB
Dendritic spine development Source: UniProtKB
Dendritic spine morphogenesis Source: UniProtKB
Detection of temperature stimulus involved in sensory perception of pain Source: UniProtKB
Ephrin receptor signaling pathway Source: UniProtKB
Establishment of cell polarity Source: UniProtKB
Immunological synapse formation Source: Ensembl
Modulation of chemical synaptic transmission Source: Ensembl
Negative regulation of satellite cell differentiation Source: UniProtKB
Negative regulation of skeletal muscle satellite cell proliferation Source: UniProtKB
Neural precursor cell proliferation Source: UniProtKB
Neurogenesis Source: UniProtKB
Optic nerve morphogenesis Source: Ensembl
Positive regulation of kinase activity Source: GO_Central
Positive regulation of synapse assembly Source: UniProtKB
Protein autophosphorylation Source: UniProtKB
Regulation of ERK1 and ERK2 cascade Source: UniProtKB
Regulation of JNK cascade Source: UniProtKB
Regulation of neuron death Source: UniProtKB
Retinal ganglion cell axon guidance Source: UniProtKB
Skeletal muscle satellite cell activation Source: UniProtKB
Transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central

Early endosome membrane; Cell membrane; Dendrite

Extracellular: 18-540
Helical: 541-563
Cytoplasmic: 564-984

Phosphorylated. Autophosphorylation is stimulated by the ligand EFNB1. Required for interaction with SH2 domain-containing interactors, for activation of the MAPK/ERK and JUN signaling cascades and for ubiquitination by CBL.
Ubiquitinated; (EFNB1)ligand-induced poly- and/or multi-ubiquitination by CBL is regulated by SRC and leads to lysosomal degradation.