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http://purl.uniprot.org/citations/17097062http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17097062http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17097062http://www.w3.org/2000/01/rdf-schema#comment"AMP-activated protein kinase (AMPK) acts as an intracellular sensor for maintaining the energy balance. Activation of AMPK switches on ATP-generating process while switches off ATP-consuming process. It achieves these effects by phosphorylation of downstream metabolic enzymes. It has been proposed that AMPK also regulates gene expression through phosphorylation of certain transcription factors; however its molecular mechanism is not fully understood. Here we show the cloning and characterization of a novel zinc finger transcription factor referred to as AREBP. AREBP is phosphorylated at Ser(470) by AMPK. Phosphorylation reduces the DNA-binding activity of AREBP. Transient transfection experiments indicate that wild-type AREBP, but not Ser(470) to Ala(470) substituted non-phosphorylating mutant, represses gene expression of the phosphoenolpyruvate carboxykinase (PEPCK), a key enzyme of gluconeogenesis. RNA interference-mediated reduction of endogenous AREBP expression attenuates AMPK-induced PEPCK down-regulation. These results implicate AREBP as a novel key modulator of PEPCK gene expression regulated by AMPK."xsd:string
http://purl.uniprot.org/citations/17097062http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2006.10.124"xsd:string
http://purl.uniprot.org/citations/17097062http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2006.10.124"xsd:string
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/author"Inoue E."xsd:string
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/author"Inoue E."xsd:string
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/author"Yamauchi J."xsd:string
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/author"Yamauchi J."xsd:string
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/pages"793-799"xsd:string
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/pages"793-799"xsd:string
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/title"AMP-activated protein kinase regulates PEPCK gene expression by direct phosphorylation of a novel zinc finger transcription factor."xsd:string
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/title"AMP-activated protein kinase regulates PEPCK gene expression by direct phosphorylation of a novel zinc finger transcription factor."xsd:string
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/volume"351"xsd:string
http://purl.uniprot.org/citations/17097062http://purl.uniprot.org/core/volume"351"xsd:string
http://purl.uniprot.org/citations/17097062http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17097062
http://purl.uniprot.org/citations/17097062http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17097062
http://purl.uniprot.org/citations/17097062http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17097062
http://purl.uniprot.org/citations/17097062http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17097062
http://purl.uniprot.org/uniprot/F6WEQ6http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17097062
http://purl.uniprot.org/uniprot/Q9BU19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17097062