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http://purl.uniprot.org/citations/22715467http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22715467http://www.w3.org/2000/01/rdf-schema#comment"Phosphatidylinositol 4,5-bisphosphate (PIP₂) is best known as a plasma membrane-bound regulatory lipid. Although PIP₂ and phosphoinositide-modifying enzymes coexist in the nucleus, their nuclear roles remain unclear. We showed that inositol polyphosphate multikinase (IPMK), which functions both as an inositol kinase and as a phosphoinositide 3-kinase (PI3K), interacts with the nuclear receptor steroidogenic factor 1 (SF-1) and phosphorylates its bound ligand, PIP₂. In vitro studies showed that PIP₂ was not phosphorylated by IPMK if PIP₂ was displaced or blocked from binding to the large hydrophobic pocket of SF-1 and that the ability to phosphorylate PIP₂ bound to SF-1 was specific to IPMK and did not occur with type 1 p110 PI3Ks. IPMK-generated SF-1-PIP₃ (phosphatidylinositol 3,4,5-trisphosphate) was dephosphorylated by the lipid phosphatase PTEN. Consistent with the in vitro activities of IPMK and PTEN on SF-1-PIP(n), SF-1 transcriptional activity was reduced by silencing IPMK or overexpressing PTEN. This ability of lipid kinases and phosphatases to directly remodel and alter the activity of a non-membrane protein-lipid complex establishes a previously unappreciated pathway for promoting lipid-mediated signaling in the nucleus."xsd:string
http://purl.uniprot.org/citations/22715467http://purl.org/dc/terms/identifier"doi:10.1126/scisignal.2003111"xsd:string
http://purl.uniprot.org/citations/22715467http://purl.uniprot.org/core/author"Suzawa M."xsd:string
http://purl.uniprot.org/citations/22715467http://purl.uniprot.org/core/author"Blind R.D."xsd:string
http://purl.uniprot.org/citations/22715467http://purl.uniprot.org/core/author"Ingraham H.A."xsd:string
http://purl.uniprot.org/citations/22715467http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22715467http://purl.uniprot.org/core/name"Sci Signal"xsd:string
http://purl.uniprot.org/citations/22715467http://purl.uniprot.org/core/pages"ra44"xsd:string
http://purl.uniprot.org/citations/22715467http://purl.uniprot.org/core/title"Direct modification and activation of a nuclear receptor-PIP(2) complex by the inositol lipid kinase IPMK."xsd:string
http://purl.uniprot.org/citations/22715467http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/22715467http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22715467
http://purl.uniprot.org/citations/22715467http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22715467
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http://purl.uniprot.org/uniprot/#_Q13285-mappedCitation-22715467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22715467
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http://purl.uniprot.org/uniprot/#_Q8NFU5-mappedCitation-22715467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22715467
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