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http://purl.uniprot.org/citations/10501226http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10501226http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10501226http://www.w3.org/2000/01/rdf-schema#comment"Phosphorylation of the glutamate receptor is an important mechanism of synaptic plasticity. Here, we show that the C terminus of GluR2 of the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptor is phosphorylated by protein kinase C and that serine-880 is the major phosphorylation site. This phosphorylation also occurs in human embryonic kidney (HEK) cells by addition of 12-O-tetradecanoylphorbol 13-acetate. Our immunoprecipitation experiment revealed that the phosphorylation of serine-880 in GluR2 drastically reduced the affinity for glutamate receptor-interacting protein (GRIP), a synaptic PDZ domain-containing protein, in vitro and in HEK cells. This result suggests that modulation of serine-880 phosphorylation in GluR2 controls the clustering of AMPA receptors at excitatory synapses and consequently contributes to synaptic plasticity."xsd:string
http://purl.uniprot.org/citations/10501226http://purl.org/dc/terms/identifier"doi:10.1046/j.1471-4159.1999.731765.x"xsd:string
http://purl.uniprot.org/citations/10501226http://purl.org/dc/terms/identifier"doi:10.1046/j.1471-4159.1999.731765.x"xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/author"Hirai H."xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/author"Hirai H."xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/author"Matsuda S."xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/author"Matsuda S."xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/author"Mikawa S."xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/author"Mikawa S."xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/name"J. Neurochem."xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/name"J. Neurochem."xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/pages"1765-1768"xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/pages"1765-1768"xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/title"Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein."xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/title"Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein."xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/volume"73"xsd:string
http://purl.uniprot.org/citations/10501226http://purl.uniprot.org/core/volume"73"xsd:string
http://purl.uniprot.org/citations/10501226http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10501226
http://purl.uniprot.org/citations/10501226http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10501226
http://purl.uniprot.org/citations/10501226http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10501226
http://purl.uniprot.org/citations/10501226http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10501226