Frederic Pincet, PhD
Associate Research Scientist in Cell BiologyCards
About
Research
Publications
2024
Dual-Ring SNAREpin Machinery Tuning for Fast Synaptic Vesicle Fusion
Caruel M, Pincet F. Dual-Ring SNAREpin Machinery Tuning for Fast Synaptic Vesicle Fusion. Biomolecules 2024, 14: 600. PMID: 38786007, PMCID: PMC11117985, DOI: 10.3390/biom14050600.Peer-Reviewed Original ResearchAuthor Correction: Kinetic study of membrane protein interactions: from three to two dimensions
Adrien V, Reffay M, Taulier N, Verchère A, Monlezun L, Picard M, Ducruix A, Broutin I, Pincet F, Urbach W. Author Correction: Kinetic study of membrane protein interactions: from three to two dimensions. Scientific Reports 2024, 14: 8222. PMID: 38589433, PMCID: PMC11001852, DOI: 10.1038/s41598-024-58201-9.Peer-Reviewed Original ResearchPhotosensitive Nanoprobes for Rapid High Purity Isolation and Size‐Specific Enrichment of Synthetic and Extracellular Vesicle Subpopulations
Weerakkody J, Tseng T, Topper M, Thoduvayil S, Radhakrishnan A, Pincet F, Kyriakides T, Gunasekara R, Ramakrishnan S. Photosensitive Nanoprobes for Rapid High Purity Isolation and Size‐Specific Enrichment of Synthetic and Extracellular Vesicle Subpopulations. Advanced Functional Materials 2024 DOI: 10.1002/adfm.202400390.Peer-Reviewed Original ResearchExtracellular vesicle subpopulationsVesicle subpopulationsIsolation of vesiclesPurity extracellular vesiclesRelease of vesiclesAnalysis of nucleic acidsNear-native formLarge-scale isolationLipid nanoprobesDownstream analysisPurity isolationEfficient isolationVesiclesSynthetic vesiclesNucleic acidsExtracellular vesiclesIsolation methodIsolatesBiomarker discoveryExposure to lightSubpopulationsEnrichmentProteinComplex biological mediaCleavageKinetic study of membrane protein interactions: from three to two dimensions
Adrien V, Reffay M, Taulier N, Verchère A, Monlezun L, Picard M, Ducruix A, Broutin I, Pincet F, Urbach W. Kinetic study of membrane protein interactions: from three to two dimensions. Scientific Reports 2024, 14: 882. PMID: 38195620, PMCID: PMC10776792, DOI: 10.1038/s41598-023-50827-5.Peer-Reviewed Original ResearchConceptsMembrane proteinsMembrane protein interactionsProtein-protein interactionsProtein complexesProtein interactionsMembrane environmentOpposite membranesBacterial efflux pumpsProtein behaviorProtein systemsMolecular interactionsEfflux pumpsProteinExploration distanceMembraneFluorescence recovery experimentsInteractionBinding rateBinding constantsComplexes
2023
A model for collagen secretion by intercompartmental continuities
Bunel L, Pincet L, Malhotra V, Raote I, Pincet F. A model for collagen secretion by intercompartmental continuities. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 121: e2310404120. PMID: 38147551, PMCID: PMC10769856, DOI: 10.1073/pnas.2310404120.Peer-Reviewed Original ResearchMembrane Tubulation with a Biomembrane Force Probe
Pincet L, Pincet F. Membrane Tubulation with a Biomembrane Force Probe. Membranes 2023, 13: 910. PMID: 38132914, PMCID: PMC10744658, DOI: 10.3390/membranes13120910.Peer-Reviewed Original ResearchBiomembrane force probeOptical tweezersForce probeTweezersGiant unilamellar vesiclesMeasurement of forcesExperimental setupMicromanipulation techniqueUnilamellar vesiclesProbeSimilar tubesMaterial transportLocal geometryHigh curvatureMicromanipulationMolecular interactionsGUVsSetupEnergeticsInteractionMeasurementsFormationTubeNanospringsApolipoproteins L1 and L3 control mitochondrial membrane dynamics
Lecordier L, Heo P, Graversen J, Hennig D, Skytthe M, d’Elzius A, Pincet F, Pérez-Morga D, Pays E. Apolipoproteins L1 and L3 control mitochondrial membrane dynamics. Cell Reports 2023, 42: 113528. PMID: 38041817, PMCID: PMC10765320, DOI: 10.1016/j.celrep.2023.113528.Peer-Reviewed Original ResearchConceptsVesicle-associated membrane protein 8Mitochondrial membrane dynamicsPI4KBMembrane dynamicsPI4KB activityMembrane protein 8Mitochondrial reactive oxygen speciesNeuronal calcium sensor-1Apolipoprotein L1C-terminal truncationsEndolysosomal membranesFission factorCalneuron-1Mitochondria fissionProhibitin 2Reactive oxygen speciesMitophagy fluxProtein 8APOL3KbOxygen speciesGolgiKB activityAPOL1MitophagySynaptophysin 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
The Get1/2 insertase forms a channel to mediate the insertion of tail-anchored proteins into the ER
Heo P, Culver J, Miao J, Pincet F, Mariappan M. The Get1/2 insertase forms a channel to mediate the insertion of tail-anchored proteins into the ER. Cell Reports 2022, 42: 111921. PMID: 36640319, PMCID: PMC9932932, DOI: 10.1016/j.celrep.2022.111921.Peer-Reviewed Original ResearchConceptsTransmembrane domainTA proteinsSingle C-terminal transmembrane domainC-terminal transmembrane domainTail-anchored (TA) proteinsTail-anchored proteinsEndoplasmic reticulum membraneGet3Reticulum membraneChannel functionInsertaseBulk fluorescenceAqueous channelsProteinChannel activityMutation analysisMembraneMicrofluidic assayTranslocaseYeastComplexesInsertionTranslocationHydrophilic segmentsBinding