2020
O-GlcNAc transferase inhibits visceral fat lipolysis and promotes diet-induced obesity
Yang Y, Fu M, Li MD, Zhang K, Zhang B, Wang S, Liu Y, Ni W, Ong Q, Mi J, Yang X. O-GlcNAc transferase inhibits visceral fat lipolysis and promotes diet-induced obesity. Nature Communications 2020, 11: 181. PMID: 31924761, PMCID: PMC6954210, DOI: 10.1038/s41467-019-13914-8.Peer-Reviewed Original ResearchMeSH KeywordsAcetylglucosamineAnimalsCell Line, TumorDietFastingGene DeletionHEK293 CellsHeLa CellsHomeostasisHumansIntra-Abdominal FatLipolysisMaleMiceMice, Inbred C3HMice, Inbred C57BLMice, KnockoutN-AcetylglucosaminyltransferasesObesityPerilipin-1PhosphorylationProtein Processing, Post-TranslationalSignal TransductionConceptsDiet-induced obesityVisceral fatExcessive visceral fat accumulationPerilipin 1Visceral fat accumulationVisceral fat lossTreatment of obesityPrimary risk factorAdipose tissue homeostasisUnhealthy obesityRisk factorsEnhanced lipolysisInhibits lipolysisFat accumulationO-GlcNAcylationFat lossObesityFat lipolysisRelated diseasesLipolysisInducible deletionLipid dropletsHexosamine biosynthetic pathwayFatTissue homeostasis
2019
O-GlcNAcase targets pyruvate kinase M2 to regulate tumor growth
Singh JP, Qian K, Lee JS, Zhou J, Han X, Zhang B, Ong Q, Ni W, Jiang M, Ruan HB, Li MD, Zhang K, Ding Z, Lee P, Singh K, Wu J, Herzog RI, Kaech S, Wendel HG, Yates JR, Han W, Sherwin RS, Nie Y, Yang X. O-GlcNAcase targets pyruvate kinase M2 to regulate tumor growth. Oncogene 2019, 39: 560-573. PMID: 31501520, PMCID: PMC7107572, DOI: 10.1038/s41388-019-0975-3.Peer-Reviewed Original ResearchMeSH KeywordsAcetylationAcetylglucosamineAnimalsAntigens, NeoplasmCarrier ProteinsCell Line, TumorDatasets as TopicDisease ProgressionFemaleGene Expression ProfilingGlycolysisHEK293 CellsHistone AcetyltransferasesHumansHyaluronoglucosaminidaseMaleMembrane ProteinsMiceN-AcetylglucosaminyltransferasesNeoplasm GradingNeoplasm StagingNeoplasmsProtein Processing, Post-TranslationalThyroid HormonesTissue Array AnalysisUp-RegulationXenograft Model Antitumor AssaysConceptsPyruvate kinase M2O-GlcNAcaseAerobic glycolysisO-GlcNAcylationKinase M2Lysine acetyltransferase activityTumor growthMetabolic rheostatAcetyltransferase activityGlcNAc transferaseMolecular basisMetabolic shiftHuman cancersGlycolysisCancer cellsHigh glucose conditionsGlucose availabilityTumor progressionGlucose conditionsExquisite controlGrowthRheostatCausative roleTargetEnzyme
2018
Adipocyte OGT governs diet-induced hyperphagia and obesity
Li MD, Vera NB, Yang Y, Zhang B, Ni W, Ziso-Qejvanaj E, Ding S, Zhang K, Yin R, Wang S, Zhou X, Fang EX, Xu T, Erion DM, Yang X. Adipocyte OGT governs diet-induced hyperphagia and obesity. Nature Communications 2018, 9: 5103. PMID: 30504766, PMCID: PMC6269424, DOI: 10.1038/s41467-018-07461-x.Peer-Reviewed Original ResearchConceptsSerine/threonine residuesN-acetylglucosamine transferaseNutrient cuesThreonine residuesTranscriptional activationO-GlcNAcylationLipid desaturationIntracellular proteinsOGTHigh-fat diet-induced hyperphagiaDevelopment of obesityBaseline food intakeSignaling contributesLipid signalsCB1 signalingBrain axisChronic dysregulationFood intakeMetabolic diseasesPalatable foodPharmacological manipulationHyperphagiaObesityFat sensorSignaling
2017
Protein O-GlcNAcylation: emerging mechanisms and functions
Yang X, Qian K. Protein O-GlcNAcylation: emerging mechanisms and functions. Nature Reviews Molecular Cell Biology 2017, 18: 452-465. PMID: 28488703, PMCID: PMC5667541, DOI: 10.1038/nrm.2017.22.Peer-Reviewed Original ResearchConceptsPost-translational modificationsO-GlcNAcylationAdaptor proteinGlcNAcylation levelsO-GlcNAc homeostasisTetratricopeptide repeat domainDiverse cellular processesProtein-protein interactionsOptimal cellular functionContext-dependent recruitmentPost-translational levelCell signaling dynamicsUnwanted protein aggregationCellular O-GlcNAcylationSubstrate-specific interactionsSpecific cell typesN-acetylglucosamine moietiesLevels of OGTGlcNAc signalingMitochondrial proteinsSpatiotemporal regulationCellular functionsCellular processesEpigenetic modificationsProtein substrates
2013
O-GlcNAc Signaling Entrains the Circadian Clock by Inhibiting BMAL1/CLOCK Ubiquitination
Li MD, Ruan HB, Hughes ME, Lee JS, Singh JP, Jones SP, Nitabach MN, Yang X. O-GlcNAc Signaling Entrains the Circadian Clock by Inhibiting BMAL1/CLOCK Ubiquitination. Cell Metabolism 2013, 17: 303-310. PMID: 23395176, PMCID: PMC3647362, DOI: 10.1016/j.cmet.2012.12.015.Peer-Reviewed Original ResearchConceptsCircadian clockProtein modificationNutrient-sensing pathwaysO-GlcNAc signalingHexosamine biosynthesis pathwayCovalent protein modificationBiosynthesis pathwayGlcNAc transferaseNutritional signalsClock oscillationsO-GlcNAcylationAberrant circadian rhythmsClock targetsOGT expressionCircadian oscillationsUbiquitinationN-acetylglucosamineNutrient fluxesMetabolic oscillationsBMAL1GenesPathwayCircadian rhythmKey mechanismClock
2012
O-GlcNAc Transferase/Host Cell Factor C1 Complex Regulates Gluconeogenesis by Modulating PGC-1α Stability
Ruan HB, Han X, Li MD, Singh JP, Qian K, Azarhoush S, Zhao L, Bennett AM, Samuel VT, Wu J, Yates JR, Yang X. O-GlcNAc Transferase/Host Cell Factor C1 Complex Regulates Gluconeogenesis by Modulating PGC-1α Stability. Cell Metabolism 2012, 16: 226-237. PMID: 22883232, PMCID: PMC3480732, DOI: 10.1016/j.cmet.2012.07.006.Peer-Reviewed Original ResearchMeSH KeywordsAnalysis of VarianceAnimalsBlotting, WesternChromatin ImmunoprecipitationChromatography, High Pressure LiquidGluconeogenesisHeat-Shock ProteinsHEK293 CellsHep G2 CellsHost Cell Factor C1HumansHyperglycemiaImmunoprecipitationLiverMiceMice, Inbred C57BLMultiprotein ComplexesN-AcetylglucosaminyltransferasesPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaProteomicsReal-Time Polymerase Chain ReactionTandem Mass SpectrometryTranscription FactorsConceptsHCF-1O-GlcNAcylationPGC-1αHost cell factor C1Hexosamine biosynthetic pathwayN-acetylglucosamine (O-GlcNAc) modificationDeubiquitinase BAP1Proteomic approachGlcNAc transferasePosttranslational modificationsNuclear proteinsBiosynthetic pathwayMaster regulatorKey regulatorFactor C1C1 complexOGTGlucose availabilityRegulatorProteinGluconeogenesisHepatic gluconeogenesisGlucose homeostasisComplexesHepatic knockdown
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