2017
Calcium-dependent O-GlcNAc signaling drives liver autophagy in adaptation to starvation
Ruan HB, Ma Y, Torres S, Zhang B, Feriod C, Heck RM, Qian K, Fu M, Li X, Nathanson MH, Bennett AM, Nie Y, Ehrlich BE, Yang X. Calcium-dependent O-GlcNAc signaling drives liver autophagy in adaptation to starvation. Genes & Development 2017, 31: 1655-1665. PMID: 28903979, PMCID: PMC5647936, DOI: 10.1101/gad.305441.117.Peer-Reviewed Original ResearchMeSH KeywordsAdaptation, BiologicalAnimalsAutophagyAutophagy-Related Protein 5Autophagy-Related Protein-1 HomologCalcium SignalingCalcium-Calmodulin-Dependent Protein Kinase Type 2Cells, CulturedGlucagonHEK293 CellsHeLa CellsHumansInositol 1,4,5-Trisphosphate ReceptorsLiverMice, Inbred C57BLN-AcetylglucosaminyltransferasesNutritional Physiological PhenomenaConceptsAMPK-dependent phosphorylationLiver autophagyN-acetylglucosamine transferaseCalmodulin-dependent kinase IICalcium/calmodulin-dependent kinase IIWhole-body homeostasisULK proteinsNutrient homeostasisKinase IICalcium signalingAutophagic fluxGenetic ablationMetabolic adaptationAutophagyStarvationOGTPhosphorylationHomeostasisMouse liverProduction of glucoseKetone bodiesAdaptationSignalingProteinTransferase
2008
Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance
Yang X, Ongusaha PP, Miles PD, Havstad JC, Zhang F, So WV, Kudlow JE, Michell RH, Olefsky JM, Field SJ, Evans RM. Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance. Nature 2008, 451: 964-969. PMID: 18288188, DOI: 10.1038/nature06668.Peer-Reviewed Original ResearchMeSH KeywordsAcetylglucosamineAnimalsCell MembraneChlorocebus aethiopsCOS CellsInsulinInsulin ResistanceLipid MetabolismLiverMaleMiceMice, Inbred C57BLN-AcetylglucosaminyltransferasesPhosphatidylinositol PhosphatesPhosphatidylinositolsPhosphorylationProtein Structure, TertiaryProtein TransportSecond Messenger SystemsConceptsO-GlcNAcSignal transductionPhosphoinositide-binding domainsPost-translational modificationsO-GlcNAc transferaseHexosamine biosynthetic pathwayInsulin signal transductionInsulin-responsive genesCellular regulationGlcNAc transferaseNutritional cuesNuclear proteinsBiosynthetic pathwayPlasma membraneProtein degradationNutrient sensorMolecular mechanismsN-acetylglucosamineTransductionPathwayTransferaseHepatic overexpressionGlucose fluxDynamic modificationMetabolic status
2002
Recruitment of O-GlcNAc Transferase to Promoters by Corepressor mSin3A Coupling Protein O-GlcNAcylation to Transcriptional Repression
Yang X, Zhang F, Kudlow JE. Recruitment of O-GlcNAc Transferase to Promoters by Corepressor mSin3A Coupling Protein O-GlcNAcylation to Transcriptional Repression. Cell 2002, 110: 69-80. PMID: 12150998, DOI: 10.1016/s0092-8674(02)00810-3.Peer-Reviewed Original ResearchMeSH KeywordsAnimal Population GroupsAnimalsCOS CellsGene Expression RegulationGene SilencingGenes, ReporterGlycoproteinsHistone DeacetylasesHumansN-AcetylglucosaminyltransferasesPromoter Regions, GeneticRepressor ProteinsSin3 Histone Deacetylase and Corepressor ComplexTranscription FactorsTranscription, GeneticTumor Cells, CulturedConceptsRNA polymerase IIPolymerase IIGlcNAc transferaseHistone deacetylationTranscription factorsN-acetylglucosamine monosaccharidesHistone deacetylase complexO-GlcNAc modificationProtein O-GlcNAcylationDeacetylase complexTranscriptional repressionThreonine residuesPrecise functional rolePosttranslational modificationsO-GlcNAcylationFunctional roleSpecific mannerMSin3AOGTPromoterDeacetylationTransferaseCorepressorTranscriptionRepression