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http://purl.uniprot.org/citations/15220471http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15220471http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15220471http://www.w3.org/2000/01/rdf-schema#comment"Longevity regulatory genes include the Forkhead transcription factor FOXO and the NAD-dependent histone deacetylase silent information regulator 2 (Sir2). Genetic studies demonstrate that Sir2 acts to extend lifespan in Caenorhabditis elegans upstream of DAF-16, a member of the FOXO family, in the insulin-like signaling pathway. However, the molecular mechanisms underlying the requirement of DAF-16 activity in Sir2-mediated longevity remain unknown. Here we show that reversible acetylation of Foxo1 (also known as FKHR), the mouse DAF-16 ortholog, modulates its transactivation function. cAMP-response element-binding protein (CREB)-binding protein binds and acetylates Foxo1 at the K242, K245, and K262 residues, the modification of which is involved in the attenuation of Foxo1 as a transcription factor. Conversely, Sir2 binds and deacetylates Foxo1 at residues acetylated by cAMP-response element-binding protein-binding protein. Sir2 is recruited to insulin response sequence-containing promoter and increases the expression of manganese superoxide dismutase and p27(kip1) in a deacetylase-activity-dependent manner. Our findings establish Foxo1 as a direct and functional target for Sir2 in mammalian systems."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0400593101"xsd:string
http://purl.uniprot.org/citations/15220471http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0400593101"xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Daitoku H."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Daitoku H."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Fukamizu A."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Fukamizu A."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Ohshima T."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Ohshima T."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Nakajima T."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Nakajima T."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Matsuzaki H."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Matsuzaki H."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Hatta M."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Hatta M."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Aratani S."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Aratani S."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Miyagishi M."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/author"Miyagishi M."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/15220471http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string