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http://purl.uniprot.org/citations/20637728http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20637728http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20637728http://www.w3.org/2000/01/rdf-schema#comment"Pancreatic and duodenal homeobox 1 (PDX1) regulates pancreatic development and mature beta-cell function. We demonstrate by mass spectrometry that serine residue at position 269 in the C-terminal domain of PDX1 is phosphorylated in beta-cells. Besides we show that the degree of phosphorylation, assessed with a phospho-Ser-269-specific antibody, is decreased by elevated glucose concentrations in both MIN6 beta-cells and primary mouse pancreatic islets. Homeodomain interacting protein kinase 2 (HIPK2) phosphorylates PDX1 in vitro; phosphate incorporation substantially decreases in PDX1 S269A mutant. Silencing of HIPK2 led to a 51+/-0.2% decrease in Ser-269 phosphorylation in MIN6 beta-cells. Mutation of Ser-269 to phosphomimetic residue glutamic acid (S269E) or de-phosphomimetic residue alanine (S269A) exerted no effect on PDX1 half-life. Instead, PDX1 S269E mutant displayed abnormal changes in subnuclear localization in response to high glucose. Our results suggest that HIPK2-mediated phosphorylation of PDX1 at Ser-269 might be a regulatory mechanism connecting signals generated by changes in extracellular glucose concentration to downstream effectors via changes in subnuclear localization of PDX1, thereby influencing islet cell differentiation and function."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2010.07.035"xsd:string
http://purl.uniprot.org/citations/20637728http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2010.07.035"xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Pinna L.A."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Pinna L.A."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Rutter G.A."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Rutter G.A."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Semplici F."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Semplici F."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Rutter J."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Rutter J."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Meggio F."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Meggio F."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Pagano M.A."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Pagano M.A."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"An R."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"An R."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"da Silva Xavier G."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"da Silva Xavier G."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Hao H.X."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Hao H.X."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Vakhshouri S."xsd:string
http://purl.uniprot.org/citations/20637728http://purl.uniprot.org/core/author"Vakhshouri S."xsd:string