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http://purl.uniprot.org/citations/9867858http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9867858http://www.w3.org/2000/01/rdf-schema#comment"Glutamate-induced phosphorylation of myristoylated alanine-rich protein kinase C substrate (MARCKS) was investigated in cultured rat hippocampal neurons. In 32P-labeled hippocampal neurons, exposure to 10 microM glutamate induced a long lasting increase in phosphorylation of MARCKS. The long lasting increase in MARCKS phosphorylation mainly required activation of the N-methyl-D-aspartate receptor. Unexpectatively, the MARCKS phosphorylation after the 10-min incubation with glutamate was not inhibited by treatment with calphostin C, a potent inhibitor for protein kinase C (PKC), or down-regulation of PKC but was largely prevented by PD098059, a selective inhibitor for mitogen-activated protein (MAP) kinase kinase. In contrast, the phosphorylation following the short exposure to glutamate was prevented by a combination of PD098059 and calphostin C. The phosphopeptide mapping and immunoblotting analyses confirmed that PKC-dependent phosphorylation of MARCKS was transient and the MAP kinase-dependent phosphorylation was relatively persistent. Investigations of the functional properties also showed that the MARCKS phosphorylation by MAP kinase regulates its calmodulin-binding ability and its interaction with F-actin as seen in the PKC-dependent phosphorylation. These results suggest that glutamate causes a long lasting increase in MARCKS phosphorylation through activation of the N-methyl-D-aspartate receptor and subsequent activation of MAP kinase in the hippocampal neurons."xsd:string
http://purl.uniprot.org/citations/9867858http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.1.408"xsd:string
http://purl.uniprot.org/citations/9867858http://purl.uniprot.org/core/author"Yamamoto H."xsd:string
http://purl.uniprot.org/citations/9867858http://purl.uniprot.org/core/author"Fukunaga K."xsd:string
http://purl.uniprot.org/citations/9867858http://purl.uniprot.org/core/author"Miyamoto E."xsd:string
http://purl.uniprot.org/citations/9867858http://purl.uniprot.org/core/author"Ohmitsu M."xsd:string
http://purl.uniprot.org/citations/9867858http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/9867858http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/9867858http://purl.uniprot.org/core/pages"408-417"xsd:string
http://purl.uniprot.org/citations/9867858http://purl.uniprot.org/core/title"Phosphorylation of myristoylated alanine-rich protein kinase C substrate by mitogen-activated protein kinase in cultured rat hippocampal neurons following stimulation of glutamate receptors."xsd:string
http://purl.uniprot.org/citations/9867858http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/9867858http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9867858
http://purl.uniprot.org/citations/9867858http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9867858
http://purl.uniprot.org/uniprot/#_P30009-mappedCitation-9867858http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9867858
http://purl.uniprot.org/uniprot/P30009http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9867858