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http://purl.uniprot.org/citations/23395175http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23395175http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23395175http://www.w3.org/2000/01/rdf-schema#comment"Posttranslational modifications play central roles in myriad biological pathways including circadian regulation. We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β. Interestingly, OGT activity is regulated by GSK3β; hence, OGT and GSK3β exhibit reciprocal regulation. Modulating O-GlcNAcylation levels alter circadian period length in both mice and Drosophila; conversely, protein O-GlcNAcylation is circadianly regulated. Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities. In addition, O-GlcNAcylation of a region in PER2 known to regulate human sleep phase (S662-S674) competes with phosphorylation of this region, and this interplay is at least partly mediated by glucose levels. Together, these results indicate that O-GlcNAcylation serves as a metabolic sensor for clock regulation and works coordinately with phosphorylation to fine-tune circadian clock."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.org/dc/terms/identifier"doi:10.1016/j.cmet.2012.12.017"xsd:string
http://purl.uniprot.org/citations/23395175http://purl.org/dc/terms/identifier"doi:10.1016/j.cmet.2012.12.017"xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Burlingame A.L."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Burlingame A.L."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Huang Y."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Huang Y."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Shokat K.M."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Shokat K.M."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Chalkley R.J."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Chalkley R.J."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Fu Y.H."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Fu Y.H."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Ptacek L.J."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Ptacek L.J."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Baer K."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Baer K."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Allen J.J."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Allen J.J."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Kaasik K."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Kaasik K."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Kissel H."xsd:string
http://purl.uniprot.org/citations/23395175http://purl.uniprot.org/core/author"Kissel H."xsd:string