2018
A liquid phase of synapsin and lipid vesicles
Milovanovic D, Wu Y, Bian X, De Camilli P. A liquid phase of synapsin and lipid vesicles. Science 2018, 361: 604-607. PMID: 29976799, PMCID: PMC6191856, DOI: 10.1126/science.aat5671.Peer-Reviewed Original ResearchConceptsSynaptic vesiclesNeurotransmitter-containing synaptic vesiclesCalmodulin-dependent protein kinase IILipid vesiclesCalcium/calmodulin-dependent protein kinase IIProtein kinase IISmall lipid vesiclesKinase IILiquid-liquid phase separationSynapsinDistinct liquid phasesVesiclesTight clusterSynapsin 1Presynaptic sitesPhosphorylationExocytosis
2001
PIP Kinase Iγ Is the Major PI(4,5)P2 Synthesizing Enzyme at the Synapse
Wenk M, Pellegrini L, Klenchin V, Di Paolo G, Chang S, Daniell L, Arioka M, Martin T, De Camilli P. PIP Kinase Iγ Is the Major PI(4,5)P2 Synthesizing Enzyme at the Synapse. Neuron 2001, 32: 79-88. PMID: 11604140, DOI: 10.1016/s0896-6273(01)00456-1.Peer-Reviewed Original ResearchConceptsSynaptojanin 1Clathrin-coated intermediatesPolyphosphoinositide phosphatase synaptojanin-1Coat recruitmentActin functionClathrin coatPositive regulatorEndocytic zonesPIPKIgammaSynthesizing enzymesRecruitmentIgammaSynapseDephosphorylationEndocytosisMajor brainElevated levelsRegulatorProteinActinEnzymeMembraneThe Eps15 C. elegans homologue EHS-1 is implicated in synaptic vesicle recycling
Salcini A, Hilliard M, Croce A, Arbucci S, Luzzi P, Tacchetti C, Daniell L, De Camilli P, Pelicci P, Di Fiore P, Bazzicalupo P. The Eps15 C. elegans homologue EHS-1 is implicated in synaptic vesicle recycling. Nature Cell Biology 2001, 3: 755-760. PMID: 11483962, DOI: 10.1038/35087075.Peer-Reviewed Original ResearchMeSH KeywordsAldicarbAnimalsAnimals, Genetically ModifiedCaenorhabditis elegansCalcium-Binding ProteinsDynaminsFluorescent Antibody TechniqueGanglia, InvertebrateGene DeletionGenes, ReporterGTP PhosphohydrolasesInsecticidesMicroscopy, ElectronMolecular Sequence DataMovement DisordersMutationNerve Tissue ProteinsNervous SystemPhenotypePhosphoproteinsProtein TransportSequence Homology, Nucleic AcidSynaptic VesiclesTemperatureConceptsSynaptic vesicle recyclingVesicle recyclingEHS-1Protein-protein interactionsMammalian Eps15Dynamin proteinsEH domainEndocytic machineryEps15Mutant formsPermissive temperatureFunctional studiesSynaptic vesiclesDynaminUncoordinated movementsPresynaptic defectsProteinPhenotypeOrthologuesCaenorhabditisWormsGenesNematodesMachineryVesicles
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 VesiclesEndophilin/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 stagesCoatMachineryInvaginationFunctional 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 evidenceProteinAssembles
1997
Amphiphysin I Is Associated with Coated Endocytic Intermediates and Undergoes Stimulation-dependent Dephosphorylation in Nerve Terminals*
Bauerfeind R, Takei K, De Camilli P. Amphiphysin I Is Associated with Coated Endocytic Intermediates and Undergoes Stimulation-dependent Dephosphorylation in Nerve Terminals*. Journal Of Biological Chemistry 1997, 272: 30984-30992. PMID: 9388246, DOI: 10.1074/jbc.272.49.30984.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcineurinDynamin IDynaminsElectrophoresis, Polyacrylamide GelEndocytosisEnzyme InhibitorsGTP PhosphohydrolasesGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Microscopy, ElectronMicrotubulesNerve Tissue ProteinsPhospholipase DPhosphoric Monoester HydrolasesPhosphorylationPresynaptic TerminalsRatsConceptsSrc homology 3Dynamin IAmphiphysin IEndocytic intermediatesCalcineurin-dependent dephosphorylationSynaptic vesicle endocytosisSynaptic vesicle exocytosisSynaptic vesicle recyclingClathrin-coated budsBurst of exocytosisAbundant presynaptic proteinElectron microscopy immunocytochemistryHomology 3Vesicle endocytosisVesicle exocytosisConstitutive phosphorylationVesicle recyclingRapid dephosphorylationOkadaic acidPhysiological partnersDephosphorylationBinding proteinPutative rolePresynaptic proteinsProteinSynaptic Vesicle Endocytosis Impaired by Disruption of Dynamin-SH3 Domain Interactions
Shupliakov O, Löw P, Grabs D, Gad H, Chen H, David C, Takei K, De Camilli P, Brodin L. Synaptic Vesicle Endocytosis Impaired by Disruption of Dynamin-SH3 Domain Interactions. Science 1997, 276: 259-263. PMID: 9092476, DOI: 10.1126/science.276.5310.259.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCell MembraneCoated Pits, Cell-MembraneDynaminsEndocytosisGTP PhosphohydrolasesHumansLampreysMicroscopy, ElectronMolecular Sequence DataNerve Tissue ProteinsProlineRecombinant Fusion ProteinsSrc Homology DomainsSynapsesSynaptic TransmissionSynaptic VesiclesConceptsSynaptic vesicle endocytosisSH3 domainVesicle endocytosisSrc homology 3 (SH3) domain-containing proteinsDomain-containing proteinsClathrin-coated pitsClathrin-mediated endocytosisSH3 binding siteAmphiphysin SH3 domainSynaptic vesicle recyclingCOOH-terminal regionDynamin bindsDynamin functionBinding partnerVesicle recyclingDomain interactionsDynamin peptidePhysiological roleEndocytosisEssential roleBinding sitesSynaptic architectureSH3DomainAmphiphysin
1987
Synaptophysin immunoreactivity and small clear vesicles in neuroendocrine cells and related tumours
Buffa R, Rindi G, Sessa F, Gini A, Capella C, Jahn R, Navone F, De Camilli P, Solcia E. Synaptophysin immunoreactivity and small clear vesicles in neuroendocrine cells and related tumours. Molecular And Cellular Probes 1987, 1: 367-381. PMID: 3134611, DOI: 10.1016/0890-8508(87)90018-1.Peer-Reviewed Original ResearchConceptsSynaptophysin immunoreactivityNeuroendocrine cellsClear vesiclesGut endocrine tumorsHuman adrenal medullaThyroid medullary carcinomaSmall clear vesiclesNon-chromaffin paragangliomaParathyroid adenomaMedullary carcinomaNeuroendocrine carcinomaNeuroendocrine tumorsCarotid bodyEndocrine tumorsGastrointestinal mucosaLung carcinoidsNerve terminalsPituitary adenomasAdrenal medullaPituitary cellsTumorsEndocrine cellsImmunoreactivityEndocrine granulesGeneral marker
1974
Structural Difference between Luminal and Lateral Plasmalemma in Pancreatic Acinar Cells
DE CAMILLI P, PELUCHETTI D, MELDOLESI J. Structural Difference between Luminal and Lateral Plasmalemma in Pancreatic Acinar Cells. Nature 1974, 248: 245-247. PMID: 4819419, DOI: 10.1038/248245b0.Peer-Reviewed Original Research