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http://purl.uniprot.org/citations/11018053http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11018053http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11018053http://www.w3.org/2000/01/rdf-schema#comment"Dendritic spines are small protrusions on the surface of dendrites that receive the vast majority of excitatory synapses. We previously showed that the cell-surface heparan sulfate proteoglycan syndecan-2 induces spine formation upon transfection into hippocampal neurons. This effect requires the COOH-terminal EFYA sequence of syndecan-2, suggesting that cytoplasmic molecules interacting with this sequence play a critical role in spine morphogenesis. Here, we report a novel protein that binds to the EFYA motif of syndecan-2. This protein, named synbindin, is expressed by neurons in a pattern similar to that of syndecan-2, and colocalizes with syndecan-2 in the spines of cultured hippocampal neurons. In transfected hippocampal neurons, synbindin undergoes syndecan-2-dependent clustering. Synbindin is structurally related to yeast proteins known to be involved in vesicle transport. Immunoelectron microscopy localized synbindin on postsynaptic membranes and intracellular vesicles within dendrites, suggesting a role in postsynaptic membrane trafficking. Synbindin coimmunoprecipitates with syndecan-2 from synaptic membrane fractions. Our results show that synbindin is a physiological syndecan-2 ligand on dendritic spines. We suggest that syndecan-2 induces spine formation by recruiting intracellular vesicles toward postsynaptic sites through the interaction with synbindin."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.org/dc/terms/identifier"doi:10.1083/jcb.151.1.53"xsd:string
http://purl.uniprot.org/citations/11018053http://purl.org/dc/terms/identifier"doi:10.1083/jcb.151.1.53"xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/author"Yamaguchi Y."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/author"Yamaguchi Y."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/author"Miura Y."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/author"Miura Y."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/author"Irie F."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/author"Irie F."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/author"Ethell I.M."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/author"Ethell I.M."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/author"Hagihara K."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/author"Hagihara K."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/pages"53-68"xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/pages"53-68"xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/title"Synbindin, a novel syndecan-2-binding protein in neuronal dendritic spines."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/title"Synbindin, a novel syndecan-2-binding protein in neuronal dendritic spines."xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/volume"151"xsd:string
http://purl.uniprot.org/citations/11018053http://purl.uniprot.org/core/volume"151"xsd:string