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http://purl.uniprot.org/citations/8052599http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8052599http://www.w3.org/2000/01/rdf-schema#comment"Insulin stimulation drives the formation of a complex between tyrosine-phosphorylated insulin receptor substrate 1 (IRS-1) and 1-phosphatidylinositol 3-kinase (PI 3-kinase; ATP:1-phosphatidyl-1D-myo-inositol 3-phosphotransferase, EC 2.7.1.137), a heterodimer consisting of regulatory 85-kDa (p85) and catalytic 110-kDa (p110) subunits. This interaction takes place via the phosphorylated YMXM motifs of IRS-1 and the Src homology region 2 (SH2) domains of p85. In this study, the stable overexpression in a Chinese hamster ovary (CHO) cell line of a mutant p85 alpha (delta p85) protein, which lacks a binding site for p110, disrupted the complex formation between IRS-1 and the catalytic subunit of PI 3-kinase in intact cells during insulin stimulation. Activation of insulin receptor kinase and the tyrosine phosphorylation of IRS-1 remained unaffected. In this cell line, both insulin-stimulated accumulation of phosphatidylinositol 3,4,5-trisphosphate and the insulin-stimulated glucose uptake due to the translocation of GLUT1 glucose transporters were markedly impaired, whereas neither phorbol 12-myristate 13-acetate-stimulated glucose uptake nor the insulin-stimulated activation of RAS was impaired. These results suggest that PI 3-kinase is required for glucose transport in insulin signaling in CHO cells."xsd:string
http://purl.uniprot.org/citations/8052599http://purl.org/dc/terms/identifier"doi:10.1073/pnas.91.16.7415"xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/author"Hara K."xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/author"Kitamura Y."xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/author"Yonezawa K."xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/author"Ando A."xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/author"Kitamura T."xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/author"Jackson T.R."xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/author"Ueda H."xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/author"Kotani K."xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/author"Sakaue H."xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/author"Stephens L."xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/pages"7415-7419"xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/title"1-Phosphatidylinositol 3-kinase activity is required for insulin-stimulated glucose transport but not for RAS activation in CHO cells."xsd:string
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/volume"91"xsd:string
http://purl.uniprot.org/citations/8052599http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8052599
http://purl.uniprot.org/citations/8052599http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8052599
http://purl.uniprot.org/citations/8052599http://purl.uniprot.org/core/authorsIncomplete"true"xsd:boolean
http://purl.uniprot.org/uniprot/P23727#attribution-78AF6054320CCF9A476EA5F5615520E0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/8052599
http://purl.uniprot.org/uniprot/P23727#attribution-AF600A20F45592B2FBA1024C2D6F2DB4http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/8052599
http://purl.uniprot.org/uniprot/P27986#attribution-98E267AF85C796A3010D6CFE5B5E6535http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/8052599