2024
A proteome-wide quantitative platform for nanoscale spatially resolved extraction of membrane proteins into native nanodiscs
Brown C, Ghosh S, McAllister R, Kumar M, Walker G, Sun E, Aman T, Panda A, Kumar S, Li W, Coleman J, Liu Y, Rothman J, Bhattacharyya M, Gupta K. A proteome-wide quantitative platform for nanoscale spatially resolved extraction of membrane proteins into native nanodiscs. Nature Methods 2024, 1-10. PMID: 39609567, DOI: 10.1038/s41592-024-02517-x.Peer-Reviewed Original ResearchTarget membrane proteinsMembrane proteinsMembrane contextSynaptic vesicle membrane proteinVesicle membrane proteinsMammalian membrane proteinsMembrane-active polymersExtraction of membrane proteinsNative nanodiscsOrganellar membranesNative membrane environmentMultiprotein complexesMolecular contextCellular membranesMembrane environmentQuantitative platformBioanalytical approachesExtraction efficiencyOpen-access databasesProteinMembraneExtraction conditionsNanodiscsTarget MPCapturing membrane snapshots: A quantitative proteome-wide guide for high-throughput spatially resolved extraction of membrane proteins for structural/functional studies on native membranes
Brown C, Ghosh S, McAllister R, Coleman J, Sun E, Zheng H, Kumar S, Panda A, Rothman J, Bhattacharyya M, Gupta K. Capturing membrane snapshots: A quantitative proteome-wide guide for high-throughput spatially resolved extraction of membrane proteins for structural/functional studies on native membranes. Biophysical Journal 2024, 123: 68a-69a. DOI: 10.1016/j.bpj.2023.11.487.Peer-Reviewed Original Research
2023
Studying Membrane Protein–Lipid Specificity through Direct Native Mass Spectrometric Analysis from Tunable Proteoliposomes
Panda A, Brown C, Gupta K. Studying Membrane Protein–Lipid Specificity through Direct Native Mass Spectrometric Analysis from Tunable Proteoliposomes. Journal Of The American Society For Mass Spectrometry 2023, 34: 1917-1927. PMID: 37432128, PMCID: PMC10932607, DOI: 10.1021/jasms.3c00110.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsMembrane proteinsNative mass spectrometryTrafficking pathwaysPlasma membraneEukaryotic integral membrane proteinsEndoplasmic reticulumBiophysical propertiesMembrane protein assemblySynaptic vesiclesCellular trafficking pathwaysOrganellar membranesLipid specificityTransmembrane proteinProtein assembliesMembrane contextMass spectrometric analysisProteinNative mass spectrometric analysesVAMP2Lipid compositionExogenous ligandsLipid membranesIndividual lipidsMembraneDirect determination of oligomeric organization of integral membrane proteins and lipids from intact customizable bilayer
Panda A, Giska F, Duncan A, Welch A, Brown C, McAllister R, Hariharan P, Goder J, Coleman J, Ramakrishnan S, Pincet F, Guan L, Krishnakumar S, Rothman J, Gupta K. Direct determination of oligomeric organization of integral membrane proteins and lipids from intact customizable bilayer. Nature Methods 2023, 20: 891-897. PMID: 37106230, PMCID: PMC10932606, DOI: 10.1038/s41592-023-01864-5.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsMembrane proteinsOligomeric organizationOligomeric stateNative mass spectrometry analysisFunctional oligomeric stateKey membrane componentMass spectrometry analysisNMS analysisTarget membraneLipid bindingMembrane componentsProteolipid vesiclesMembrane compositionLipid compositionSpectrometry analysisLipid membranesNeurotransmitter releaseProteinMembraneLipidsMembrane propertiesDirect determinationBilayersTransporters
2022
A Quantitative Native Mass Spectrometry Platform for Deconstructing Hierarchical Organization of Membrane Proteins and Lipids
Panda A, Giska F, Brown C, Coleman J, Rothman J, Gupta K. A Quantitative Native Mass Spectrometry Platform for Deconstructing Hierarchical Organization of Membrane Proteins and Lipids. The FASEB Journal 2022, 36 DOI: 10.1096/fasebj.2022.36.s1.0r472.Peer-Reviewed Original ResearchMembrane proteinsOligomeric stateSpecific lipidsBiophysical propertiesSugar transporter proteinsPhysiological membranesBacterial plasma membraneTarget membrane proteinsLipid bilayer environmentSynaptic vesicle proteinsLipid compositionMS/MS capabilitiesProtein oligomerizationCellular signalingOligomeric organizationVesicle proteinsMembrane curvaturePlasma membraneMacromolecular assembliesTransporter proteinsNative massOligomeric populationMS/MS analysisRegulatory roleDiverse setA tunable lipid bilayer native MS platform for direct determination of hierarchical organization of membrane proteins and lipids at the membrane
Panda A, Giska F, Brown C, Coleman J, Rothman J, Gupta K. A tunable lipid bilayer native MS platform for direct determination of hierarchical organization of membrane proteins and lipids at the membrane. Biophysical Journal 2022, 121: 312a-313a. DOI: 10.1016/j.bpj.2021.11.1192.Peer-Reviewed Original Research