2024
Analysis of Mucin‐Domain Glycoproteins Using Mass Spectrometry
Mahoney K, Malaker S. Analysis of Mucin‐Domain Glycoproteins Using Mass Spectrometry. Current Protocols 2024, 4: e1100. PMID: 38984456, PMCID: PMC11239139, DOI: 10.1002/cpz1.1100.Peer-Reviewed Original ResearchGlycoproteomics: Charting new territory in mass spectrometry and glycobiology
Malaker S. Glycoproteomics: Charting new territory in mass spectrometry and glycobiology. Journal Of Mass Spectrometry 2024, 59: e5034. PMID: 38726698, DOI: 10.1002/jms.5034.Peer-Reviewed Original Research
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 factor
2022
Cell-specific bioorthogonal tagging of glycoproteins
Cioce A, Calle B, Rizou T, Lowery SC, Bridgeman VL, Mahoney KE, Marchesi A, Bineva-Todd G, Flynn H, Li Z, Tastan OY, Roustan C, Soro-Barrio P, Rafiee MR, Garza-Garcia A, Antonopoulos A, Wood TM, Keenan T, Both P, Huang K, Parmeggian F, Snijders AP, Skehel M, Kjær S, Fascione MA, Bertozzi CR, Haslam SM, Flitsch SL, Malaker SA, Malanchi I, Schumann B. Cell-specific bioorthogonal tagging of glycoproteins. Nature Communications 2022, 13: 6237. PMID: 36284108, PMCID: PMC9596482, DOI: 10.1038/s41467-022-33854-0.Peer-Reviewed Original ResearchConceptsMass spectrometry glycoproteomicsArtificial biosynthetic pathwayTumor-derived cell linesCellular model systemNon-transfected cellsCellular functionsProtein glycosylationBiosynthetic pathwayProteome analysisGlycosylation sitesBioorthogonal tagsCancer developmentCell linesModel systemImportant modulatorIntricate interactionsCo-culture modelGlycoproteinCellsGlycoprotein expressionMouse modelGlycoproteomeGlycosylationTaggingMonocultureGlycoproteomics
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 fieldProteinGlycansSpectrometryCurrent strategies for characterization of mucin-domain glycoproteins
Ince D, Lucas TM, Malaker SA. Current strategies for characterization of mucin-domain glycoproteins. Current Opinion In Chemical Biology 2022, 69: 102174. PMID: 35752002, DOI: 10.1016/j.cbpa.2022.102174.Peer-Reviewed Original ResearchConceptsGlycopeptide mimeticsPost-translational modificationsCurrent characterization techniquesCellular glycosylation pathwaysSynthetic methodCharacterization techniquesGlycosylation pathwayMucin domainO-glycosylationBiological functionsGlycoproteomic workflowGlycosylationGlycoproteinExciting avenuesRecent breakthroughsMucin glycoproteinsRecent developments
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 subtypeRoleCellsMetabolic precision labeling enables selective probing of O-linked N-acetylgalactosamine glycosylation
Debets MF, Tastan OY, Wisnovsky SP, Malaker SA, Angelis N, Moeckl LKR, Choi J, Flynn H, Wagner LJS, Bineva-Todd G, Antonopoulos A, Cioce A, Browne WM, Li Z, Briggs DC, Douglas HL, Hess GT, Agbay AJ, Roustan C, Kjaer S, Haslam SM, Snijders AP, Bassik MC, Moerner WE, Li VSW, Bertozzi CR, Schumann B. Metabolic precision labeling enables selective probing of O-linked N-acetylgalactosamine glycosylation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 25293-25301. PMID: 32989128, PMCID: PMC7568240, DOI: 10.1073/pnas.2007297117.Peer-Reviewed Original ResearchConceptsStructure-based design processN-acetylgalactosamine glycosylationProtein glycosylation eventsCell surface glycoproteomeCRISPR knockout screensMetabolic labeling experimentsGlycan subtypesGlycosylation eventsSecretory pathwayGalNAc glycosylationProtein glycosylationEctopic expressionSer/GalNAc-T2Superresolution microscopyGlycan typesLiving cellsBioorthogonal tagsGlycosylationIntestinal organoidsMetabolic interconversionSuch specificityUridine diphosphateLabeling experimentsCells