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
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