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http://purl.uniprot.org/citations/12177059http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12177059http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12177059http://www.w3.org/2000/01/rdf-schema#comment"3-Phosphoinositide-dependent protein kinase-1 (PDK1) plays a central role in activating the protein kinase A, G, and C subfamily. In particular, PDK1 plays an important role in regulating the Akt survival pathway by phosphorylating Akt on Thr-308. PDK1 kinase activity was thought to be constitutively active; however, recent reports suggested that its activity is regulated by binding to other proteins, such as protein kinase C-related kinase-2 (PRK2), p90 ribosomal protein S6 kinase-2 (RSK2), and heat-shock protein 90 (Hsp90). Here we report that PDK1 binds to 14-3-3 proteins in vivo and in vitro through the sequence surrounding Ser-241, a residue that is phosphorylated by itself and is critical for its kinase activity. Mutation of PDK1 to increase its binding to 14-3-3 decreased its kinase activity in vivo. By contrast, mutation of PDK1 to decrease its interaction with 14-3-3 resulted in increased PDK1 kinase activity. Moreover, incubation of wild-type PDK1 with recombinant 14-3-3 in vitro decreased its kinase activity. These data indicate that PDK1 kinase activity is negatively regulated by binding to 14-3-3 through the PDK1 autophosphorylation site Ser-241."xsd:string
http://purl.uniprot.org/citations/12177059http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m205141200"xsd:string
http://purl.uniprot.org/citations/12177059http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m205141200"xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/author"Fujita N."xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/author"Fujita N."xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/author"Sato S."xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/author"Sato S."xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/author"Tsuruo T."xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/author"Tsuruo T."xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/pages"39360-39367"xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/pages"39360-39367"xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/title"Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3."xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/title"Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3."xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/12177059http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/12177059http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12177059
http://purl.uniprot.org/citations/12177059http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12177059
http://purl.uniprot.org/citations/12177059http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12177059
http://purl.uniprot.org/citations/12177059http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12177059