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http://purl.uniprot.org/citations/17681146http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17681146http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17681146http://www.w3.org/2000/01/rdf-schema#comment"The family of mammalian Sirtuin proteins comprises seven members homologous to yeast Sir2. Here we show that SIRT2, a cytoplasmic sirtuin, is the most abundant sirtuin in adipocytes. Sirt2 expression is downregulated during preadipocyte differentiation in 3T3-L1 cells. Overexpression of SIRT2 inhibits differentiation, whereas reducing SIRT2 expression promotes adipogenesis. Both effects are accompanied by corresponding changes in the expression of PPARgamma, C/EBPalpha, and genes marking terminal adipocyte differentiation, including Glut4, aP2, and fatty acid synthase. The mechanism underlying the effects of reduced SIRT2 in 3T3-L1 adipocytes includes increased acetylation of FOXO1, with direct interaction between SIRT2 and FOXO1. This interaction enhances insulin-stimulated phosphorylation of FOXO1, which in turn regulates FOXO1 nuclear and cytosolic localization. Thus, Sirt2 acts as an important regulator of adipocyte differentiation through modulation of FOXO1 acetylation/phosphorylation and activity and may play a role in controlling adipose tissue mass and function."xsd:string
http://purl.uniprot.org/citations/17681146http://purl.org/dc/terms/identifier"doi:10.1016/j.cmet.2007.07.003"xsd:string
http://purl.uniprot.org/citations/17681146http://purl.org/dc/terms/identifier"doi:10.1016/j.cmet.2007.07.003"xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/author"Kahn C.R."xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/author"Kahn C.R."xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/author"Gesta S."xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/author"Gesta S."xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/author"Jing E."xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/author"Jing E."xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/name"Cell Metab."xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/name"Cell Metab."xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/pages"105-114"xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/pages"105-114"xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/title"SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation."xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/title"SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation."xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/17681146http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/17681146http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17681146
http://purl.uniprot.org/citations/17681146http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17681146
http://purl.uniprot.org/citations/17681146http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17681146
http://purl.uniprot.org/citations/17681146http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17681146