2024
VPS13B 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 ResearchMeSH KeywordsAnimalsBrefeldin AGolgi ApparatusHeLa CellsHumansProtein BindingProtein TransportVesicular Transport ProteinsZebrafishZebrafish ProteinsConceptsLipid transportGolgi complex proteinGolgi subcompartmentsGolgi membranesGolgi cisternaeProtein familyFunctional partnersGolgi complexKO cellsComplex proteinsFAM177A1GolgiVPS13BAdjacent membranesMutationsProteinCohen syndromeLipidOrthologsInteractorsBrefeldinMembraneOrganellesSubcompartmentsDevelopmental disorders
2022
A partnership between the lipid scramblase XK and the lipid transfer protein VPS13A at the plasma membrane
Guillén-Samander A, Wu Y, Pineda SS, García FJ, Eisen JN, Leonzino M, Ugur B, Kellis M, Heiman M, De Camilli P. A partnership between the lipid scramblase XK and the lipid transfer protein VPS13A at the plasma membrane. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2205425119. PMID: 35994651, PMCID: PMC9436381, DOI: 10.1073/pnas.2205425119.Peer-Reviewed Original ResearchMeSH KeywordsCarrier ProteinsCell MembraneEndoplasmic ReticulumHumansLipidsNeuroacanthocytosisVesicular Transport ProteinsConceptsCaudate neuronsClinical manifestationsExposure of PtdSerPH domainMcLeod syndromeCell surface exposureER-PM contactsLipid dropletsTransport of lipidsPutative roleUnknown mechanismNeuronsLipid transfer proteinVPS13ALipid scramblasesTransfer proteinCytosolic loopExposurePlasma membraneCell surfaceEndoplasmic reticulumLipid transferERSyndromeDisease
2021
Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport
Leonzino M, Reinisch KM, De Camilli P. Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport. Biochimica Et Biophysica Acta (BBA) - Molecular And Cell Biology Of Lipids 2021, 1866: 159003. PMID: 34216812, PMCID: PMC8325632, DOI: 10.1016/j.bbalip.2021.159003.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutophagosomesAutophagy-Related ProteinsCryoelectron MicroscopyDisease Models, AnimalEukaryotic CellsHeredodegenerative Disorders, Nervous SystemHumansHydrophobic and Hydrophilic InteractionsLipid BilayersLipid MetabolismMitochondrial MembranesMutationProtein DomainsStructure-Activity RelationshipVesicular Transport ProteinsYeastsConceptsLipid transportMembrane contact sitesDomain protein familyOccurrence of proteinsVPS13 proteinsEukaryotic cellsNumerous proteinsProtein familyIntracellular membranesProtein bridgeHydrophobic grooveContact sitesMembrane growthLipid transferBilayer lipidsNovel mechanismVps13New mechanismProteinLipidsAtg2OrganellesAdjacent bilayersDiscoveryMechanism
2020
Role of VPS13, a protein with similarity to ATG2, in physiology and disease
Ugur B, Hancock-Cerutti W, Leonzino M, De Camilli P. Role of VPS13, a protein with similarity to ATG2, in physiology and disease. Current Opinion In Genetics & Development 2020, 65: 61-68. PMID: 32563856, PMCID: PMC7746581, DOI: 10.1016/j.gde.2020.05.027.Peer-Reviewed Original ResearchMeSH KeywordsAutophagy-Related ProteinsBrainHumansNeurodegenerative DiseasesNeurodevelopmental DisordersVesicular Transport ProteinsConceptsAutophagy protein ATG2N-terminal halfVPS13 proteinsMolecular functionsCellular processesFamily proteinsVps13Contact sitesAtg2Intracellular organellesFunctional studiesNovel mechanismProteinSimilar roleHydrophobic channelStructural studiesNeurodegenerative disordersPhysiologyDirect transferOrganellesSimilarityMutationsRoleLipidsBilayers
2018
VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites
Kumar N, Leonzino M, Hancock-Cerutti W, Horenkamp FA, Li P, Lees JA, Wheeler H, Reinisch KM, De Camilli P. VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites. Journal Of Cell Biology 2018, 217: 3625-3639. PMID: 30093493, PMCID: PMC6168267, DOI: 10.1083/jcb.201807019.Peer-Reviewed Original ResearchConceptsN-terminal portionAutophagy protein ATG2Membrane lipid homeostasisLate endosomes/lysosomesSecondary structure similarityLipid transport proteinsER contact sitesEndosomes/lysosomesHuman VPS13AVPS13 genesVps13Implicating defectsTransport proteinsLipid transportersContact sitesGenetic studiesLipid homeostasisLipid exchangeTransport roleProteinOrganellesVPS13ANeurodegenerative disordersStructure similarityHydrophobic cavity
2016
Endosome-ER Contacts Control Actin Nucleation and Retromer Function through VAP-Dependent Regulation of PI4P
Dong R, Saheki Y, Swarup S, Lucast L, Harper JW, De Camilli P. Endosome-ER Contacts Control Actin Nucleation and Retromer Function through VAP-Dependent Regulation of PI4P. Cell 2016, 166: 408-423. PMID: 27419871, PMCID: PMC4963242, DOI: 10.1016/j.cell.2016.06.037.Peer-Reviewed Original Research
2000
Synaptic Autoimmunity and the Salk Factor
Solimena M, De Camilli P. Synaptic Autoimmunity and the Salk Factor. Neuron 2000, 28: 309-316. PMID: 11144336, DOI: 10.1016/s0896-6273(00)00105-7.Peer-Reviewed Original ResearchEpsin 1 Undergoes Nucleocytosolic Shuttling and Its Eps15 Interactor Nh2-Terminal Homology (Enth) Domain, Structurally Similar to Armadillo and Heat Repeats, Interacts with the Transcription Factor Promyelocytic Leukemia Zn2+ Finger Protein (Plzf)
Hyman J, Chen H, Di Fiore P, De Camilli P, Brunger A. Epsin 1 Undergoes Nucleocytosolic Shuttling and Its Eps15 Interactor Nh2-Terminal Homology (Enth) Domain, Structurally Similar to Armadillo and Heat Repeats, Interacts with the Transcription Factor Promyelocytic Leukemia Zn2+ Finger Protein (Plzf). Journal Of Cell Biology 2000, 149: 537-546. PMID: 10791968, PMCID: PMC2174850, DOI: 10.1083/jcb.149.3.537.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsArmadillo Domain ProteinsBeta CateninCalcium-Binding ProteinsCarrier ProteinsCell LineCell NucleusCrystallography, X-RayCytoskeletal ProteinsCytosolDNA-Binding ProteinsDrosophila ProteinsFluorescent Antibody TechniqueInsect ProteinsModels, MolecularMolecular Sequence DataNeuropeptidesPhosphoproteinsProtein BindingRatsSequence AlignmentTrans-ActivatorsTranscription FactorsVesicular Transport ProteinsZinc FingersConceptsENTH domainFinger proteinCRM1-dependent nuclear export pathwayClathrin adaptor AP-2Nuclear export pathwayAdaptor AP-2HEAT repeatsEndocytic machineryNuclear functionsHomology domainExport pathwayLeptomycin BEpsin 1AP-2Cytosolic proteinsUnknown functionDirect interactionEpsinTerminal portionClathrinProteinArmadillosAntifungal antibioticsPathwayDomain
1999
The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein Module*
Rosenthal J, Chen H, Slepnev V, Pellegrini L, Salcini A, Di Fiore P, De Camilli P. The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein Module*. Journal Of Biological Chemistry 1999, 274: 33959-33965. PMID: 10567358, DOI: 10.1074/jbc.274.48.33959.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsCalcium-Binding ProteinsCarrier ProteinsCHO CellsClathrinCoated VesiclesCricetinaeDNA, ComplementaryFluorescent Antibody TechniqueGene ExpressionHumansIntracellular Signaling Peptides and ProteinsLuciferasesMaleMembrane ProteinsMolecular Sequence DataNeuropeptidesPhosphoproteinsPhylogenyProtein BindingProtein Structure, TertiaryRatsRecombinant Fusion ProteinsSequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidTissue DistributionVesicular Transport ProteinsConceptsEpsin 1Clathrin coatClathrin adaptor AP-2New protein modulesNew protein familyTerminal regionAdaptor AP-2Family of proteinsRat brain libraryNPF motifsProtein modulesProtein familyCell peripheryAP-2Membrane dynamicsSimilar proteinsBrain libraryClathrinEps15Vesicle fractionEpsinGreen fluorescentGolgi regionCell surfaceProteinTetanus Toxin Blocks the Exocytosis of Synaptic Vesicles Clustered at Synapses But Not of Synaptic Vesicles in Isolated Axons
Verderio C, Coco S, Bacci A, Rossetto O, De Camilli P, Montecucco C, Matteoli M. Tetanus Toxin Blocks the Exocytosis of Synaptic Vesicles Clustered at Synapses But Not of Synaptic Vesicles in Isolated Axons. Journal Of Neuroscience 1999, 19: 6723-6732. PMID: 10436029, PMCID: PMC6782867, DOI: 10.1523/jneurosci.19-16-06723.1999.Peer-Reviewed Original ResearchEpidermal growth factor pathway substrate 15, Eps15
Salcini A, Chen H, Iannolo G, De Camilli P, Di Fiore P. Epidermal growth factor pathway substrate 15, Eps15. The International Journal Of Biochemistry & Cell Biology 1999, 31: 805-809. PMID: 10481267, DOI: 10.1016/s1357-2725(99)00042-4.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsCalcium-Binding ProteinsCarrier ProteinsCell LineChromosomes, Human, Pair 1EndocytosisEpidermal Growth FactorHumansIntracellular Signaling Peptides and ProteinsNeuropeptidesPhosphoproteinsSignal TransductionTransferrinVesicular Transport ProteinsConceptsEpidermal growth factor receptorPutative coiled-coil regionCoiled-coil regionCell proliferationNIH 3T3 cellsReceptor-mediated endocytosisEH domainNH2-terminal portionEndocytic machineryEpsin functionIntracellular sortingEps15Growth factor receptorTerminal domainAP-2Kinase activityBinding proteinMultiple copiesBiomolecular strategiesProteinFactor receptorTripartite structureMLL geneGenesProliferationThe Interaction of Epsin and Eps15 with the Clathrin Adaptor AP-2 Is Inhibited by Mitotic Phosphorylation and Enhanced by Stimulation-dependent Dephosphorylation in Nerve Terminals*
Chen H, Slepnev V, Di Fiore P, De Camilli P. The Interaction of Epsin and Eps15 with the Clathrin Adaptor AP-2 Is Inhibited by Mitotic Phosphorylation and Enhanced by Stimulation-dependent Dephosphorylation in Nerve Terminals*. Journal Of Biological Chemistry 1999, 274: 3257-3260. PMID: 9920862, DOI: 10.1074/jbc.274.6.3257.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsBase SequenceCalcium-Binding ProteinsCarrier ProteinsCell LineDNA PrimersEndocytosisExocytosisIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceMitosisNerve EndingsNeuropeptidesPhosphoproteinsPhosphorylationProtein BindingRatsVesicular Transport Proteins
1998
Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis
Chen H, Fre S, Slepnev V, Capua M, Takei K, Butler M, Di Fiore P, De Camilli P. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis. Nature 1998, 394: 793-797. PMID: 9723620, DOI: 10.1038/29555.Peer-Reviewed Original ResearchAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsBlotting, NorthernBrainCalcium-Binding ProteinsCarrier ProteinsCHO CellsClathrinCricetinaeEndocytosisMembrane ProteinsMolecular Sequence DataNeuropeptidesPhosphoproteinsProtein BindingRatsRecombinant Fusion ProteinsTransfectionVesicular Transport Proteins
1997
Identification and characterization of homologues of the Exocyst component Sec10p
Guo W, Roth D, Gatti E, De Camilli P, Novick P. Identification and characterization of homologues of the Exocyst component Sec10p. FEBS Letters 1997, 404: 135-139. PMID: 9119050, DOI: 10.1016/s0014-5793(97)00109-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCloning, MolecularCOS CellsExocytosisFungal ProteinsGolgi ApparatusHumansMammalsMolecular Sequence DataPolymerase Chain ReactionRecombinant ProteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTranscription, GeneticTransfectionVesicular Transport ProteinsConceptsC. elegans proteinsCharacterization of homologuesAmino acid identityBroad tissue distributionGolgi trafficMammalian counterpartsYeast SaccharomycesAcid identityGene productsCOS cellsWestern blot analysisSec10pPeripheral cytoplasmExocystBlot analysisProteinTissue distributionImmunofluorescence stainingSec8pCellsSaccharomycesCloningHomologuesExocytosisCytoplasm
1996
Yeast protein translocation complex: Isolation of two genes SEB1 and SEB2 encoding proteins homologous to the Sec61β subunit
Toikkanen J, Gatti E, Takei K, Saloheimo M, Olkkonen V, Söderlund H, De Camilli P, Keränen S. Yeast protein translocation complex: Isolation of two genes SEB1 and SEB2 encoding proteins homologous to the Sec61β subunit. Yeast 1996, 12: 425-438. PMID: 8740416, DOI: 10.1002/(sici)1097-0061(199604)12:5<425::aid-yea924>3.0.co;2-b.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBiological TransportCell LineChlorocebus aethiopsCloning, MolecularCytoplasmDNA, ComplementaryDogsEndoplasmic ReticulumFungal ProteinsGenes, FungalGenes, SuppressorMembrane ProteinsMembrane Transport ProteinsMicrosomesMolecular Sequence DataMolecular WeightSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSEC Translocation ChannelsSequence Analysis, DNASequence Homology, Amino AcidVesicular Transport ProteinsConceptsBeta subunitN-terminal signal sequencePotential membrane-spanning regionsEndoplasmic reticulumProtein translocation apparatusMembrane-spanning regionNovel genetic toolsTemperature-sensitive phenotypeHydrophilic N-terminusEvolutionary conservationTranslocation apparatusYeast genesHeterologous hybridizationProtein translocationHomologous genesER membraneGenetic toolsSignal sequenceChromosomal disruptionMulticopy plasmidC-terminusDouble disruptionN-terminusFunctional analysisSeb1The V o Sector of the V-ATPase, Synaptobrevin, and Synaptophysin Are Associated on Synaptic Vesicles in a Triton X-100-resistant, Freeze-thawing Sensitive, Complex (∗)
Galli T, McPherson P, De Camilli P. The V o Sector of the V-ATPase, Synaptobrevin, and Synaptophysin Are Associated on Synaptic Vesicles in a Triton X-100-resistant, Freeze-thawing Sensitive, Complex (∗). Journal Of Biological Chemistry 1996, 271: 2193-2198. PMID: 8567678, DOI: 10.1074/jbc.271.4.2193.Peer-Reviewed Original Research
1994
Synaptic targeting of rabphilin-3A, a synaptic vesicle Ca2+/phospholipid-binding protein, depends on rab3A/3C
Li C, Takei K, Geppert M, Daniell L, Stenius K, Chapman E, Jahn R, De Camilli P, Südhof T. Synaptic targeting of rabphilin-3A, a synaptic vesicle Ca2+/phospholipid-binding protein, depends on rab3A/3C. Neuron 1994, 13: 885-898. PMID: 7946335, DOI: 10.1016/0896-6273(94)90254-2.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsBase SequenceBiological EvolutionBrain ChemistryConserved SequenceDNA, ComplementaryFluorescent Antibody TechniqueGlutathione TransferaseGTP-Binding ProteinsMiceMice, Mutant StrainsMicroscopy, ImmunoelectronMolecular Sequence DataNerve Tissue ProteinsNeuronsRab GTP-Binding ProteinsRab3 GTP-Binding ProteinsRatsRecombinant Fusion ProteinsVesicular Transport ProteinsConceptsGTP-dependent mannerSynaptic vesicle membraneRabphilin-3AVesicle membraneLow molecular weight GTPPeripheral membrane proteinsSynaptic vesiclesSynaptic vesicle dockingRab3A-deficient miceSynaptic vesicle proteinsMembrane recruitmentVesicle dockingPutative functionsMembrane proteinsWeight GTPVesicle proteinsN-terminusSynaptic targetingRab3CRab3AProteinVesiclesMembraneSynaptic patternsNormal levelsThe role of Rab3A in neurotransmitter release
Geppert M, Bolshakov V, Siegelbaum S, Takei K, De Camilli P, Hammer R, Südhof T. The role of Rab3A in neurotransmitter release. Nature 1994, 369: 493-497. PMID: 7911226, DOI: 10.1038/369493a0.Peer-Reviewed Original ResearchConceptsRole of Rab3ASynaptic vesicle exocytosisSmall GTPRab3A geneHomologous recombinationVesicle exocytosisSynaptic vesiclesHippocampal CA1 pyramidal cellsSynaptic proteinsProteinCA1 pyramidal cellsNeurotransmitter releaseExocytosisGTPPyramidal cellsRepetitive stimulationSynaptic depressionElectrophysiological recordingsRepetitive stimuliCompensatory changesShort trainsRabphilinRab3Rab3AGenes