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http://purl.uniprot.org/citations/15886229http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15886229http://www.w3.org/2000/01/rdf-schema#comment"AMP-activated protein kinase (AMPK) regulates both glycogen and lipid metabolism functioning as an intracellular energy sensor. In this study, we identified a 160-kDa protein in mouse skeletal muscle lysate by using a glutathione-S-transferase (GST)-AMPK fusion protein pull-down assay. Mass spectrometry and a Mascot search revealed this protein to be a glycogen debranching enzyme (GDE). The association between AMPK and GDE was observed not only in the overexpression system but also endogenously. Next, we showed the beta1-subunit of AMPK to be responsible for the association with GDE. Furthermore, experiments using deletion mutants of the beta1-subunit of AMPK revealed amino acids 68-123 of the beta1-subunit to be sufficient for GDE binding. W100G and K128Q, both beta1-subunit mutants, are reportedly incapable of binding to glycogen, but both bound GDE, indicating that the association between AMPK and GDE does not involve glycogen. Rather, the AMPK-GDE association is likely to be direct. Overexpression of amino acids 68-123 of the beta1-subunit inhibited the association between endogenous AMPK and GDE. Although GDE activity was unaffected, basal phosphorylation and kinase activity of AMPK, as well as phosphorylation of acetyl-CoA carboxylase, were significantly increased. Thus it is likely that the AMPK-GDE association is a novel mechanism regulating AMPK activity and the resultant fatty acid oxidation and glucose uptake."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.org/dc/terms/identifier"doi:10.1152/ajpendo.00003.2005"xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Anai M."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Ogihara T."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Ono H."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Kurihara H."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Sakoda H."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Kikuchi M."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Asano T."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Fujishiro M."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Fukushima Y."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Horike N."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Shojima N."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Uchijima Y."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Kushiyama A."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Viana A.Y."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/author"Fujio J."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/name"Am J Physiol Endocrinol Metab"xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/pages"E474-81"xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/title"Glycogen debranching enzyme association with beta-subunit regulates AMP-activated protein kinase activity."xsd:string
http://purl.uniprot.org/citations/15886229http://purl.uniprot.org/core/volume"289"xsd:string
http://purl.uniprot.org/citations/15886229http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15886229
http://purl.uniprot.org/citations/15886229http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15886229