Yumei Wu, PhD
Research ScientistCards
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Research
Publications
2025
BLTP3A is associated with membranes of the late endocytic pathway and is an effector of CASM
Hanna M, Rodriguez Cruz H, Fujise K, Wu Y, Xu C, Pang S, Li Z, Monetti M, De Camilli P. BLTP3A is associated with membranes of the late endocytic pathway and is an effector of CASM. The EMBO Journal 2025, 1-28. PMID: 40935891, DOI: 10.1038/s44318-025-00543-9.Peer-Reviewed Original ResearchMultiple interactions recruit BLTP2 to ER-PM contacts to control plasma membrane dynamics
Dai A, Xu P, Amos C, Fujise K, Wu Y, Yang H, Eisen J, Guillén-Samander A, De Camilli P. Multiple interactions recruit BLTP2 to ER-PM contacts to control plasma membrane dynamics. Journal Of Cell Biology 2025, 224: e202504027. PMID: 40899996, PMCID: PMC12406788, DOI: 10.1083/jcb.202504027.Peer-Reviewed Original ResearchConceptsPlasma membraneTubular endosomesN-BAR domain proteinsER-PM contactsPlasma membrane dynamicsLipid transport functionLipid transfer proteinsDomain proteinsMembrane dynamicsN-BARLipid transportTransfer proteinCell typesEndosomesIntracellular vacuolesProteinTransport functionPM dynamicsMacropinosomesAdaptorMultiple interactionsLipidPhosphoinositideERVacuolesTriglycerides are an important fuel reserve for synapse function in the brain
Kumar M, Wu Y, Knapp J, Pontius C, Park D, Witte R, McAllister R, Gupta K, Rajagopalan K, De Camilli P, Ryan T. Triglycerides are an important fuel reserve for synapse function in the brain. Nature Metabolism 2025, 7: 1392-1403. PMID: 40595405, PMCID: PMC12286841, DOI: 10.1038/s42255-025-01321-x.Peer-Reviewed Original ResearchConceptsLipid dropletsFatty acidsMitochondrial ATP productionFunction in vivoActivity-dependent fashionNerve terminalsATP productionNeuronal function in vivoSynapse functionAdult male miceTriglyceride lipaseIn vivo neuronsDDHD2Neuronal bioenergeticsMale miceAcute blockElectrical silenceMetabolic supportNeuronsNerveFuel reservesElectrical activityMitochondriaCognitive functionBioenergetics
2024
Ectopic reconstitution of a spine-apparatus-like structure provides insight into mechanisms underlying its formation
Falahati H, Wu Y, Fang M, De Camilli P. Ectopic reconstitution of a spine-apparatus-like structure provides insight into mechanisms underlying its formation. Current Biology 2024, 35: 265-276.e4. PMID: 39626668, PMCID: PMC11753949, DOI: 10.1016/j.cub.2024.11.010.Peer-Reviewed Original ResearchEndoplasmic reticulumSpine apparatusActin bundlesEndomembrane networkER sheetsConserved regionProtein synaptopodinCisternal organelleNon-neuronal cellsER cisternsOrganellesSynaptopodinProteinNeuronal dendritesNeuronal spinesAxon initial segmentFindings shed lightBiogenesisActinProtein matrixNarrow lumenReticulumMammalsInitial segmentMechanismVPS13B is localized at the interface between Golgi cisternae and is a functional partner of FAM177A1
Ugur B, Schueder F, Shin J, Hanna M, Wu Y, Leonzino M, Su M, McAdow A, Wilson C, Postlethwait J, Solnica-Krezel L, Bewersdorf J, De Camilli P. VPS13B is localized at the interface between Golgi cisternae and is a functional partner of FAM177A1. Journal Of Cell Biology 2024, 223: e202311189. PMID: 39331042, PMCID: PMC11451052, DOI: 10.1083/jcb.202311189.Peer-Reviewed Original ResearchConceptsLipid transportGolgi complex proteinGolgi subcompartmentsGolgi membranesGolgi cisternaeProtein familyFunctional partnersGolgi complexKO cellsComplex proteinsFAM177A1GolgiVPS13BAdjacent membranesMutationsProteinCohen syndromeLipidOrthologsInteractorsBrefeldinMembraneOrganellesSubcompartmentsDevelopmental disordersAbsence of ATG9A and synaptophysin demixing on Rab5 mutation-induced giant endosomes
Choi J, Wu Y, Park D. Absence of ATG9A and synaptophysin demixing on Rab5 mutation-induced giant endosomes. Molecular Brain 2024, 17: 63. PMID: 39223639, PMCID: PMC11367939, DOI: 10.1186/s13041-024-01132-3.Peer-Reviewed Original ResearchConceptsGiant endosomesFormation of enlarged endosomesAutophagy-related (ATG) proteinsPool of vesiclesIntegral membrane proteinsRab5 mutantsEnlarged endosomesCore autophagy-related (ATG) proteinsEndosomal localizationIntracellular sortingMembrane proteinsEndocytic originEndosomesATG9ARab5ProteinVesiclesMutantsSegregation mechanismSynapsinCo-assemblyNerve terminalsSynaptophysinFibroblastsCellsOverlapping role of synaptophysin and synaptogyrin family proteins in determining the small size of synaptic vesicles
Park D, Fujise K, Wu Y, Luján R, Del Olmo-Cabrera S, Wesseling J, De Camilli P. Overlapping role of synaptophysin and synaptogyrin family proteins in determining the small size of synaptic vesicles. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2409605121. PMID: 38985768, PMCID: PMC11260120, DOI: 10.1073/pnas.2409605121.Peer-Reviewed Original ResearchConceptsSynaptic vesiclesFamily proteinsBiogenesis of synaptic vesiclesClusters of small vesiclesSize of synaptic vesiclesSynaptogyrin familySynaptogyrin-1Vesicle proteinsSynaptogyrinTransmembrane domainOrganismal levelSmall vesiclesProteinMild defectsVesiclesFamily membersBiogenesisSmall sizeFamilyMiceSynapsinCoexpressionAbundanceSynaptoporinMembers
2023
Mutations in Parkinsonism-linked endocytic proteins synaptojanin1 and auxilin have synergistic effects on dopaminergic axonal pathology
Ng X, Wu Y, Lin Y, Yaqoob S, Greene L, De Camilli P, Cao M. Mutations in Parkinsonism-linked endocytic proteins synaptojanin1 and auxilin have synergistic effects on dopaminergic axonal pathology. Npj Parkinson's Disease 2023, 9: 26. PMID: 36792618, PMCID: PMC9932162, DOI: 10.1038/s41531-023-00465-5.Peer-Reviewed Original ResearchParkinson's diseaseMutant miceStriatal nerve terminalsSingle mutant miceDouble mutant miceDAergic markersDAergic terminalsAtypical parkinsonismDAergic neuronsStriatal interneuronsNeurological manifestationsAxonal pathologyDopaminergic inputNerve terminalsSynaptojanin 1Dystrophic changesPD pathogenesisKnockout miceRisk proteinsSynaptic defectsNeurodegenerative disordersParkinsonismMiceAdaptive changesDiseaseSynaptic vesicle proteins and ATG9A self-organize in distinct vesicle phases within synapsin condensates
Park D, Wu Y, Wang X, Gowrishankar S, Baublis A, De Camilli P. Synaptic vesicle proteins and ATG9A self-organize in distinct vesicle phases within synapsin condensates. Nature Communications 2023, 14: 455. PMID: 36709207, PMCID: PMC9884207, DOI: 10.1038/s41467-023-36081-3.Peer-Reviewed Original ResearchConceptsMembrane proteinsSV membrane proteinsVesicle membrane proteinEctopic expression systemSynaptic vesicle proteinsSynaptic vesicle clustersSV proteinsVesicle proteinsEctopic expressionExpression systemVesicle clustersSynapsinProteinLiquid-like propertiesVesiclesDistinct classesDual roleSynapsin 1FibroblastsATG9ASynapsesExpressionDistinct phasesNerve terminalsClusters
2022
Proximity proteomics of synaptopodin provides insight into the molecular composition of the spine apparatus of dendritic spines
Falahati H, Wu Y, Feuerer V, Simon HG, De Camilli P. Proximity proteomics of synaptopodin provides insight into the molecular composition of the spine apparatus of dendritic spines. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2203750119. PMID: 36215465, PMCID: PMC9586327, DOI: 10.1073/pnas.2203750119.Peer-Reviewed Original ResearchConceptsSpine apparatusDendritic spinesSubset of neuronsAxon initial segmentDendritic shaftsER cisternsNonneuronal cellsSynaptopodinSpineSmooth endoplasmic reticulumEndoplasmic reticulumCisternal organelleInitial segmentSpecific localizationCisternsBinding proteinPDLIM7Expression patternsSubsetProteinSmall subsetDiseaseNeuronsBrainFunctional partnership
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