2022
Presynaptic autophagy is coupled to the synaptic vesicle cycle via ATG-9
Yang S, Park D, Manning L, Hill SE, Cao M, Xuan Z, Gonzalez I, Dong Y, Clark B, Shao L, Okeke I, Almoril-Porras A, Bai J, De Camilli P, Colón-Ramos DA. Presynaptic autophagy is coupled to the synaptic vesicle cycle via ATG-9. Neuron 2022, 110: 824-840.e10. PMID: 35065714, PMCID: PMC9017068, DOI: 10.1016/j.neuron.2021.12.031.Peer-Reviewed Original ResearchConceptsSynaptic vesicle cycleVesicle cyclePresynaptic autophagyAutophagosome biogenesisATG-9Only transmembrane proteinTrans-Golgi networkCellular degradation pathwayPresynaptic sitesActivity-dependent mannerTransmembrane proteinSynaptojanin 1Synaptic fociBiogenesisAutophagyNeuronal healthDegradation pathwayTraffickingPathwayParkinson's diseaseSynaptic activityNeuronal activityElegansSitesEndocytosis
2021
Cooperative function of synaptophysin and synapsin in the generation of synaptic vesicle-like clusters in non-neuronal cells
Park D, Wu Y, Lee SE, Kim G, Jeong S, Milovanovic D, De Camilli P, Chang S. Cooperative function of synaptophysin and synapsin in the generation of synaptic vesicle-like clusters in non-neuronal cells. Nature Communications 2021, 12: 263. PMID: 33431828, PMCID: PMC7801664, DOI: 10.1038/s41467-020-20462-z.Peer-Reviewed Original ResearchConceptsNon-neuronal cellsSV clustersSynaptic vesiclesSmall synaptic-like microvesiclesSV membrane proteinsSynaptic-like microvesiclesSV proteinsDiffuse cytosolic distributionMembrane proteinsReconstitution systemCytosolic distributionCooperative functionSuch vesiclesMechanistic insightsLiquid-like propertiesPowerful modelPhysiological formationProteinSynapsinVesiclesCellsSynaptic transmissionAssembly of structuresDefining featureLiquid condensate
2017
Parkinson Sac Domain Mutation in Synaptojanin 1 Impairs Clathrin Uncoating at Synapses and Triggers Dystrophic Changes in Dopaminergic Axons
Cao M, Wu Y, Ashrafi G, McCartney AJ, Wheeler H, Bushong EA, Boassa D, Ellisman MH, Ryan TA, De Camilli P. Parkinson Sac Domain Mutation in Synaptojanin 1 Impairs Clathrin Uncoating at Synapses and Triggers Dystrophic Changes in Dopaminergic Axons. Neuron 2017, 93: 882-896.e5. PMID: 28231468, PMCID: PMC5340420, DOI: 10.1016/j.neuron.2017.01.019.Peer-Reviewed Original ResearchConceptsDopaminergic axonsEarly-onset parkinsonism patientsEndocytic dysfunctionNeurological manifestationsParkinsonism patientsDystrophic changesParkinson's diseaseDorsal striatumHuman patientsClathrin-coated intermediatesParkin levelsHomozygous mutationMutant brainsSynaptojanin 1Domain mutationsTerminal changesPatientsStriking accumulationAxonsDiseaseMiceSynapsesSynaptic vesicle endocytosisMutationsDysfunction
2008
[Selective role of dynamin1 in synaptic vesicle endocytosis].
Hayashi-Nishino M, De Camilli P. [Selective role of dynamin1 in synaptic vesicle endocytosis]. Protein (Tokyo) 2008, 53: 2225-30. PMID: 21038613.Peer-Reviewed Original Research
2004
Impaired PtdIns(4,5)P2 synthesis in nerve terminals produces defects in synaptic vesicle trafficking
Paolo G, Moskowitz HS, Gipson K, Wenk MR, Voronov S, Obayashi M, Flavell R, Fitzsimonds RM, Ryan TA, Camilli P. Impaired PtdIns(4,5)P2 synthesis in nerve terminals produces defects in synaptic vesicle trafficking. Nature 2004, 431: 415-422. PMID: 15386003, DOI: 10.1038/nature02896.Peer-Reviewed Original ResearchMeSH KeywordsAction PotentialsAnimalsBiological TransportCells, CulturedClathrinElectric ConductivityEndocytosisExocytosisGene DeletionKineticsMiceMice, KnockoutNeuronsPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)Presynaptic TerminalsSynaptic TransmissionSynaptic VesiclesConceptsClathrin coat dynamicsSynaptic vesicle cycleSynaptic vesicle exocytosisSynaptic vesicle traffickingSecond messenger moleculesEarly postnatal lethalityEndocytic intermediatesVesicle traffickingMembrane proteinsVesicle cycleVesicle exocytosisPostnatal lethalityCell regulationRecycling kineticsMessenger moleculesBiochemical studiesSynaptic defectsDirect interactionImportant functionsCritical roleMultiple stepsReleasable poolRegulationNerve terminalsDephosphorylation
2001
Chronic Blockade of Glutamate Receptors Enhances Presynaptic Release and Downregulates the Interaction between Synaptophysin-Synaptobrevin–Vesicle-Associated Membrane Protein 2
Bacci A, Coco S, Pravettoni E, Schenk U, Armano S, Frassoni C, Verderio C, De Camilli P, Matteoli M. Chronic Blockade of Glutamate Receptors Enhances Presynaptic Release and Downregulates the Interaction between Synaptophysin-Synaptobrevin–Vesicle-Associated Membrane Protein 2. Journal Of Neuroscience 2001, 21: 6588-6596. PMID: 11517248, PMCID: PMC6763110, DOI: 10.1523/jneurosci.21-17-06588.2001.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedDown-RegulationEndocytosisExcitatory Amino Acid AntagonistsExcitatory Postsynaptic PotentialsExocytosisHippocampusMacromolecular SubstancesMembrane ProteinsNeuronsPatch-Clamp TechniquesPresynaptic TerminalsProtein BindingRatsReceptors, GlutamateReceptors, N-Methyl-D-AspartateR-SNARE ProteinsSynaptic TransmissionSynaptic VesiclesSynaptophysinTetrodotoxinConceptsGlutamate receptorsSynapse formationSynaptic vesicle recyclingMiniature EPSC frequencyGlutamate receptor blockersGlutamatergic nerve terminalsNumber of synapsesUptake of antibodiesVesicle recyclingChronic blockadeReceptor blockersEPSC frequencyPresynaptic releaseNerve terminalsHippocampal neuronsPresynaptic functionPostsynaptic functionChronic exposureChronic presenceInterneuronal signalingNeuronal culturesNeuronal circuitsMembrane protein 2Intracellular perfusionPrimary culturesEndocytosis and Signaling An Inseparable Partnership
Di Fiore P, De Camilli P. Endocytosis and Signaling An Inseparable Partnership. Cell 2001, 106: 1-4. PMID: 11461694, DOI: 10.1016/s0092-8674(01)00428-7.Peer-Reviewed Original Research
2000
Accessory factors in clathrin-dependent synaptic vesicle endocytosis
Slepnev V, De Camilli P. Accessory factors in clathrin-dependent synaptic vesicle endocytosis. Nature Reviews Neuroscience 2000, 1: 161-172. PMID: 11257904, DOI: 10.1038/35044540.Peer-Reviewed Original ResearchConceptsAccessory factorsNumerous accessory proteinsSynaptic vesicle endocytosisClathrin-mediated endocytosisRecent structural studiesPlasma membrane componentsSynaptic vesicle recyclingInternalization of receptorsVesicle endocytosisCoat assemblyExtracellular ligandsClathrin coatMolecular detailsVesicle recyclingAccessory proteinsGenetic studiesEndocytosisMembrane componentsSurface proteinsClathrinStructural studiesProteinVesiclesInternalizationNew aspects
1999
Essential Role of Phosphoinositide Metabolism in Synaptic Vesicle Recycling
Cremona O, Di Paolo G, Wenk M, Lüthi A, Kim W, Takei K, Daniell L, Nemoto Y, Shears S, Flavell R, McCormick D, De Camilli P. Essential Role of Phosphoinositide Metabolism in Synaptic Vesicle Recycling. Cell 1999, 99: 179-188. PMID: 10535736, DOI: 10.1016/s0092-8674(00)81649-9.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell-Free SystemCerebral CortexCoated Pits, Cell-MembraneEndocytosisEnzyme InhibitorsExonsHippocampusIn Vitro TechniquesMembrane PotentialsMiceMice, KnockoutMicroscopy, ElectronNerve EndingsNerve Tissue ProteinsNeuronsPhosphatidylinositolsPhosphoric Monoester HydrolasesSynaptic VesiclesThe Calcineurin-Dynamin 1 Complex as a Calcium Sensor for Synaptic Vesicle Endocytosis*
Lai M, Hong J, Ruggiero A, Burnett P, Slepnev V, De Camilli P, Snyder S. The Calcineurin-Dynamin 1 Complex as a Calcium Sensor for Synaptic Vesicle Endocytosis*. Journal Of Biological Chemistry 1999, 274: 25963-25966. PMID: 10473536, DOI: 10.1074/jbc.274.37.25963.Peer-Reviewed Original ResearchConceptsCalcium sensorEndocytic coat proteinsSynaptic endocytic machinerySynaptic vesicle endocytosisSynaptic vesiclesCalcium-dependent phosphatase calcineurinEndocytic machineryVesicle endocytosisDynamin 1Phosphatase calcineurinCoat proteinCalcium-dependent formationCalcium-sensing mechanismPhysical associationEndocytosisVesiclesCalcium-dependent processesClathrinSynaptotagminComplexesExocytosisCalcineurinMachineryProteinEndophilin/SH3p4 Is Required for the Transition from Early to Late Stages in Clathrin-Mediated Synaptic Vesicle Endocytosis
Ringstad N, Gad H, Löw P, Di Paolo G, Brodin L, Shupliakov O, De Camilli P. Endophilin/SH3p4 Is Required for the Transition from Early to Late Stages in Clathrin-Mediated Synaptic Vesicle Endocytosis. Neuron 1999, 24: 143-154. PMID: 10677033, DOI: 10.1016/s0896-6273(00)80828-4.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsAntibodiesCaenorhabditis elegansCarrier ProteinsCell-Free SystemClathrinCoated Pits, Cell-MembraneDynaminsEndocytosisGTP PhosphohydrolasesLampreysMicroscopy, ElectronMolecular Sequence DataRatsSpinal CordSrc Homology DomainsSynapsesSynaptic VesiclesConceptsSynaptic vesicle endocytosisVesicle endocytosisClathrin coatClathrin-coated pitsSynaptic vesicle recyclingCell-free systemEndophilin functionGTPase dynaminFunctional partnersVesicle fissionBiochemical machineryVesicle recyclingSH3p4EndophilinDynaminEndocytosisAntibody-mediated disruptionProteinActive zoneSynaptojaninClathrinLater stagesCoatMachineryInvaginationAP-2 Recruitment to Synaptotagmin Stimulated by Tyrosine-Based Endocytic Motifs
Haucke V, De Camilli P. AP-2 Recruitment to Synaptotagmin Stimulated by Tyrosine-Based Endocytic Motifs. Science 1999, 285: 1268-1271. PMID: 10455054, DOI: 10.1126/science.285.5431.1268.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAnimalsBinding SitesCalcium-Binding ProteinsCattleCell MembraneCHO CellsClathrinCoated Pits, Cell-MembraneCricetinaeEndocytosisMembrane GlycoproteinsMembrane ProteinsNerve Tissue ProteinsNeuronsOligopeptidesPhospholipase DProtein BindingRatsRecombinant Fusion ProteinsSynaptic MembranesSynaptotagminsTyrosineConceptsAP-2 recruitmentEndocytic motifAP-2Cargo proteinsPlasma membraneTyrosine-based endocytic motifClathrin adaptor protein AP-2Adaptor protein AP-2Nucleation of clathrinNon-neuronal cellsProtein synaptotagminDocking siteSynaptotagminClathrinMotifProteinRecruitmentMembraneEndocytosisTyrosineBindingCellsPeptidesEpidermal 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 geneGenesProliferationFunctional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
Takei K, Slepnev V, Haucke V, De Camilli P. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nature Cell Biology 1999, 1: 33-39. PMID: 10559861, DOI: 10.1038/9004.Peer-Reviewed Original ResearchConceptsDynamin 1Functional partnershipCell-free systemAmphiphysin 1Clathrin coatDynaminAmphiphysinRing-like structurePresence of GTPSynaptic vesiclesEndocytosisNarrow tubulesLipid bilayersMorphological evidenceBilayer curvatureVesiclesSpherical liposomesPotential functionClathrinGTPDirect morphological evidenceProteinAssemblesThe 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
Role of Phosphorylation in Regulation of the Assembly of Endocytic Coat Complexes
Slepnev V, Ochoa G, Butler M, Grabs D, De Camilli P. Role of Phosphorylation in Regulation of the Assembly of Endocytic Coat Complexes. Science 1998, 281: 821-824. PMID: 9694653, DOI: 10.1126/science.281.5378.821.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Protein Complex beta SubunitsAdaptor Proteins, Vesicular TransportAdenosine TriphosphateAnimalsBinding SitesCarbazolesChromatography, AffinityClathrinCyclosporineDimerizationDynamin IDynaminsEndocytosisEnzyme InhibitorsGTP PhosphohydrolasesIndole AlkaloidsMembrane ProteinsNerve Tissue ProteinsPhosphoric Monoester HydrolasesRatsRecombinant Fusion ProteinsSrc Homology DomainsEpsin 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 ProteinsEndocytosis proteins and cancer: a potential link?
Floyd S, De Camilli P. Endocytosis proteins and cancer: a potential link? Trends In Cell Biology 1998, 8: 299-301. PMID: 9704404, DOI: 10.1016/s0962-8924(98)01316-6.Peer-Reviewed Original ResearchConceptsEndocytosis proteinsVariety of proteinsHuman haematopoietic malignanciesReceptor-mediated endocytosisAbnormal expressionClathrin adaptorsBiology of cancerChromosomal rearrangementsHuman cancersProteinHaematopoietic malignanciesRecent studiesPotential mechanismsExpressionPotential linkClathrinEndocytosisGenesAdaptorBiologyMutationsRearrangementCancerTargetDynamin and its partners: a progress report
Schmid S, McNiven M, De Camilli P. Dynamin and its partners: a progress report. Current Opinion In Cell Biology 1998, 10: 504-512. PMID: 9719872, DOI: 10.1016/s0955-0674(98)80066-5.Peer-Reviewed Original ResearchGeneration of Coated Intermediates of Clathrin-Mediated Endocytosis on Protein-Free Liposomes
Takei K, Haucke V, Slepnev V, Farsad K, Salazar M, Chen H, De Camilli P. Generation of Coated Intermediates of Clathrin-Mediated Endocytosis on Protein-Free Liposomes. Cell 1998, 94: 131-141. PMID: 9674434, DOI: 10.1016/s0092-8674(00)81228-3.Peer-Reviewed Original Research