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http://purl.uniprot.org/citations/14500912http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14500912http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14500912http://www.w3.org/2000/01/rdf-schema#comment"Hepatocyte nuclear factors 3 alpha, beta, and gamma (Foxa-1, -2, and -3) are transcriptional activators of important metabolic genes in the liver that are suppressed by the actions of insulin. Here, we show that the activation of phosphatidylinositol 3-kinase-Akt by insulin induces Foxa-2 phosphorylation, nuclear exclusion, and inhibition of Foxa-2-dependent transcriptional activity. Foxa-2 physically interacts with Akt, a key mediator of the phosphatidylinositol 3-kinase pathway and is phosphorylated at a single conserved site (T156) that is absent in Foxa-1 and Foxa-3 proteins. This Akt phosphorylation site in Foxa-2 is highly conserved from mammals to insects. Mutant Foxa-2T156A is resistant to Akt-mediated phosphorylation, nuclear exclusion, and transcriptional inactivation of Foxa-2-regulated gene expression. These results implicate an evolutionarily conserved mechanism in the regulation of Foxa-2-dependent transcriptional control by extracellular signals such as insulin."xsd:string
http://purl.uniprot.org/citations/14500912http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1931483100"xsd:string
http://purl.uniprot.org/citations/14500912http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1931483100"xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/author"Stoffel M."xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/author"Stoffel M."xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/author"Wolfrum C."xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/author"Wolfrum C."xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/author"Besser D."xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/author"Besser D."xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/author"Luca E."xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/author"Luca E."xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/pages"11624-11629"xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/pages"11624-11629"xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/title"Insulin regulates the activity of forkhead transcription factor Hnf-3beta/Foxa-2 by Akt-mediated phosphorylation and nuclear/cytosolic localization."xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/title"Insulin regulates the activity of forkhead transcription factor Hnf-3beta/Foxa-2 by Akt-mediated phosphorylation and nuclear/cytosolic localization."xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/volume"100"xsd:string
http://purl.uniprot.org/citations/14500912http://purl.uniprot.org/core/volume"100"xsd:string
http://purl.uniprot.org/citations/14500912http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14500912
http://purl.uniprot.org/citations/14500912http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14500912