2023
Synaptophysin chaperones the assembly of 12 SNAREpins under each ready-release vesicle
Bera M, Radhakrishnan A, Coleman J, Sundaram R, Ramakrishnan S, Pincet F, Rothman J. Synaptophysin chaperones the assembly of 12 SNAREpins under each ready-release vesicle. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2311484120. PMID: 37903271, PMCID: PMC10636311, DOI: 10.1073/pnas.2311484120.Peer-Reviewed Original ResearchConceptsSpecific molecular functionsSynaptic vesicle protein synaptophysinTarget membrane bilayerSensor synaptotagminSNARE proteinsMolecular functionsMembrane proteinsSNAREpinsReceptor vesiclesSingle-molecule measurementsGene knockoutMembrane bilayerLipid bilayersProtein synaptophysinVesiclesDetergent extractsHexamer structureSYPMechanism of actionProteinAssemblyChaperonesSynaptotagminExocytosisBilayersDirect 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