2023
Glycoproteomic landscape and structural dynamics of TIM family immune checkpoints enabled by mucinase SmE
Chongsaritsinsuk J, Steigmeyer A, Mahoney K, Rosenfeld M, Lucas T, Smith C, Li A, Ince D, Kearns F, Battison A, Hollenhorst M, Judy Shon D, Tiemeyer K, Attah V, Kwon C, Bertozzi C, Ferracane M, Lemmon M, Amaro R, Malaker S. Glycoproteomic landscape and structural dynamics of TIM family immune checkpoints enabled by mucinase SmE. Nature Communications 2023, 14: 6169. PMID: 37794035, PMCID: PMC10550946, DOI: 10.1038/s41467-023-41756-y.Peer-Reviewed Original ResearchConceptsFamily of proteinsMucin domainO-glycosylationBiological functionsKey regulatorComplex glycansMass spectrometric analysisFunctional relevanceTIM familyDetailed molecular structureCritical roleGlycosylationProteinSpectrometric analysisStructural featuresUnique abilityStructural dynamicsMolecular dynamics simulationsTim-3 functionFamilyPowerful workflowRegulatorImmune cellsCheckpointGlycansComprehensive analysis of platelet glycoprotein Ibα ectodomain glycosylation
Hollenhorst M, Tiemeyer K, Mahoney K, Aoki K, Ishihara M, Lowery S, Rangel-Angarita V, Bertozzi C, Malaker S. Comprehensive analysis of platelet glycoprotein Ibα ectodomain glycosylation. Journal Of Thrombosis And Haemostasis 2023, 21: 995-1009. PMID: 36740532, PMCID: PMC10065957, DOI: 10.1016/j.jtha.2023.01.009.Peer-Reviewed Original ResearchConceptsO-glycositesGPIb-IX-V complexMajor ligand-binding subunitAmino acid sitesLigand-binding subunitVon Willebrand factor bindingPlatelet glycoprotein IbαMechanosensory domainFactor bindingEndogenous proteinsRecombinant proteinsN-glycositesStructural rolePlatelet biologyGlycan structuresGlycoprotein IbαO-glycansT antigenGlycosylation profileDiverse repertoireGlycosylationGlycansComprehensive analysisGlycositesVon Willebrand factorBump-and-hole engineering of human polypeptide N-acetylgalactosamine transferases to dissect their protein substrates and glycosylation sites in cells
Calle B, Gonzalez-Rodriguez E, Mahoney K, Cioce A, Bineva-Todd G, Tastan O, Roustan C, Flynn H, Malaker S, Schumann B. Bump-and-hole engineering of human polypeptide N-acetylgalactosamine transferases to dissect their protein substrates and glycosylation sites in cells. STAR Protocols 2023, 4: 101974. PMID: 36633947, PMCID: PMC9843269, DOI: 10.1016/j.xpro.2022.101974.Peer-Reviewed Original ResearchConceptsProtein substratesGlycosylation sitesGalNAc-T familyTransfection of cellsIndividual glycosyltransferasesBioorthogonal reportersN-acetylgalactosamine transferaseSubstrate specificityBiological functionsGalNAc-TsDisease relevanceMolecular biologyComplete detailsGlycosyltransferasesTransferaseCellsBiosynthesisBiologyReporterTransfectionGlycansSubstrateEnzymeHole engineeringSites
2022
Glycoproteomics
Bagdonaite I, Malaker S, Polasky D, Riley N, Schjoldager K, Vakhrushev S, Halim A, Aoki-Kinoshita K, Nesvizhskii A, Bertozzi C, Wandall H, Parker B, Thaysen-Andersen M, Scott N. Glycoproteomics. Nature Reviews Methods Primers 2022, 2: 48. DOI: 10.1038/s43586-022-00128-4.Peer-Reviewed Original ResearchGlycan structuresMass spectrometryPost-translational additionIntact glycopeptide analysisSite of modificationProtein glycosylationProtein modificationBioinformatics platformBiological processesGlycopeptide analysisMS fragmentationGlycoproteomic methodsGlycoproteomicsGlycosylationProtein isolationProteolytic digestionPeptide sequencesSystem-wide contextStudy of glycopeptidesPrimersRecent advancesExciting fieldProteinGlycansSpectrometry
2021
Small RNAs are modified with N-glycans and displayed on the surface of living cells
Flynn RA, Pedram K, Malaker SA, Batista PJ, Smith BAH, Johnson AG, George BM, Majzoub K, Villalta PW, Carette JE, Bertozzi CR. Small RNAs are modified with N-glycans and displayed on the surface of living cells. Cell 2021, 184: 3109-3124.e22. PMID: 34004145, PMCID: PMC9097497, DOI: 10.1016/j.cell.2021.04.023.Peer-Reviewed Original ResearchConceptsLiving cellsGlycan biosynthetic machineryDomains of lifeMultiple cell typesRNA biologySmall RNAsExtracellular biologyBiosynthetic machineryBiochemical approachesMammalian speciesBattery of chemicalAnti-dsRNA antibodiesN-glycansCell typesReceptor familyCultured cellsCell surfaceRNAThird scaffoldGlycoRNABiologyMajor targetGlycosylationGlycansSialic acid
2020
Generating orthogonal glycosyltransferase and nucleotide sugar pairs as next-generation glycobiology tools
Cioce A, Malaker SA, Schumann B. Generating orthogonal glycosyltransferase and nucleotide sugar pairs as next-generation glycobiology tools. Current Opinion In Chemical Biology 2020, 60: 66-78. PMID: 33125942, PMCID: PMC7955280, DOI: 10.1016/j.cbpa.2020.09.001.Peer-Reviewed Original ResearchConceptsMass spectrometry glycoproteomicsCell surface glycoproteomeProtein glycosylationBiological processesQuantitative biologyMutant glycosyltransferasesGlycoproteomicsDifferent glycansGlycansPrecision toolsGlycosyltransferasesBiosynthesisGlycoproteomeGlycomeGlycosyltransferaseBiologyGlycosylationGlycobiologyLabeling reagentLimited specificityPhysiologySpecificityParticular subtypeRoleCells