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http://purl.uniprot.org/citations/19427337http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19427337http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19427337http://www.w3.org/2000/01/rdf-schema#comment"The regulatory function of caveolin-2 in signal transducer and activator of transcription 3 (STAT3) signaling by insulin was investigated. Insulin-induced increase in phosphorylation of STAT3 was reduced by caveolin-2 siRNA. Mutagenesis studies identified that phosphorylation of tyrosines 19 and 27 on caveolin-2 is required for the STAT3 activation. Caveolin-2 Y27A mutation decreased insulin-induced phosphorylation of STAT3 interacting with caveolin-2. pY27-Caveolin-2 was required for nuclear translocation of pY705-STAT3 in response to insulin. In contrast, caveolin-2 Y19A mutation influenced neither the phosphorylation of STAT3 nor nuclear translocation of pY705-STAT3. pY19-Caveolin-2, however, was essential for insulin-induced DNA binding of pS727-STAT3 and STAT3-targeted gene induction in the nucleus. Finally, insulin-induced transcriptional activation of STAT3 depended on phosphorylation of both 19 and 27 tyrosines. Together, our data reveal that phosphotyrosine-caveolin-2 is a novel regulator for transcriptional activation of STAT3 in response to insulin."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.org/dc/terms/identifier"doi:10.1016/j.bbamcr.2009.04.015"xsd:string
http://purl.uniprot.org/citations/19427337http://purl.org/dc/terms/identifier"doi:10.1016/j.bbamcr.2009.04.015"xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Jeong K."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Jeong K."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Pak Y."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Pak Y."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Kwon H."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Kwon H."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Hwang E.M."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Hwang E.M."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Park J.-Y."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Park J.-Y."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Choi W.-S."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Choi W.-S."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Hong S.-G."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/author"Hong S.-G."xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/pages"1325-1333"xsd:string
http://purl.uniprot.org/citations/19427337http://purl.uniprot.org/core/pages"1325-1333"xsd:string