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http://purl.uniprot.org/citations/20348923http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20348923http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20348923http://www.w3.org/2000/01/rdf-schema#comment"Class Ia phosphoinositide 3-kinase (PI3K), an essential mediator of the metabolic actions of insulin, is composed of a catalytic (p110alpha or p110beta) and regulatory (p85alphaalpha, p85betaalpha or p55alpha) subunit. Here we show that p85alphaalpha interacts with X-box-binding protein-1 (XBP-1), a transcriptional mediator of the unfolded protein response (UPR), in an endoplasmic reticulum (ER) stress-dependent manner. Cell lines with knockout or knockdown of p85alphaalpha show marked alterations in the UPR, including reduced ER stress-dependent accumulation of nuclear XBP-1, decreased induction of UPR target genes and increased rates of apoptosis. This is associated with a decreased activation of inositol-requiring protein-1alpha (IRE1alpha) and activating transcription factor-6alphaalpha (ATF6alpha). Mice with deletion of p85alpha in liver (L-Pik3r1(-/-)) show a similar attenuated UPR after tunicamycin administration, leading to an increased inflammatory response. Thus, p85alphaalpha forms a previously unrecognized link between the PI3K pathway, which is central to insulin action, and the regulation of the cellular response to ER stress, a state that when unresolved leads to insulin resistance."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.org/dc/terms/identifier"doi:10.1038/nm.2121"xsd:string
http://purl.uniprot.org/citations/20348923http://purl.org/dc/terms/identifier"doi:10.1038/nm.2121"xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/author"Kahn C.R."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/author"Kahn C.R."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/author"Ueki K."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/author"Ueki K."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/author"Boucher J."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/author"Boucher J."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/author"Mori M.A."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/author"Mori M.A."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/author"Winnay J.N."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/author"Winnay J.N."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/name"Nat. Med."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/name"Nat. Med."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/pages"438-445"xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/pages"438-445"xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/title"A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box-binding protein-1 to modulate the unfolded protein response."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/title"A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box-binding protein-1 to modulate the unfolded protein response."xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/volume"16"xsd:string
http://purl.uniprot.org/citations/20348923http://purl.uniprot.org/core/volume"16"xsd:string