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 aspectsTandem Arrangement of the Clathrin and AP-2 Binding Domains in Amphiphysin 1 and Disruption of Clathrin Coat Function by Amphiphysin Fragments Comprising These Sites*
Slepnev V, Ochoa G, Butler M, De Camilli P. Tandem Arrangement of the Clathrin and AP-2 Binding Domains in Amphiphysin 1 and Disruption of Clathrin Coat Function by Amphiphysin Fragments Comprising These Sites*. Journal Of Biological Chemistry 2000, 275: 17583-17589. PMID: 10748223, DOI: 10.1074/jbc.m910430199.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsBinding SitesBinding, CompetitiveCHO CellsClathrinCricetinaeGlutathione TransferaseHumansMembrane ProteinsMolecular Sequence DataMonomeric Clathrin Assembly ProteinsMutagenesis, Site-DirectedNerve Tissue ProteinsPeptide FragmentsRecombinant Fusion ProteinsTransfectionConceptsAP-2Amphiphysin 1Coat proteinClathrin adaptor AP-2COOH-terminal SH3 domainAdaptor AP-2Chinese hamster ovary cellsCoat functionMultifunctional adaptorSH3 domainHamster ovary cellsTerminal domainBinding domainsClathrinDynaminMembrane lipidsAmphiphysinSynaptic vesiclesAmino acidsSynaptojaninOvary cellsDirect interactionProteinTertiary complexTandem arrangementEpsin 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 antibioticsPathwayDomainDirect interaction of the 170 kDa isoform of synaptojanin 1 with clathrin and with the clathrin adaptor AP-2
Haffner C, Di Paolo G, Rosenthal J, De Camilli P. Direct interaction of the 170 kDa isoform of synaptojanin 1 with clathrin and with the clathrin adaptor AP-2. Current Biology 2000, 10: 471-474. PMID: 10801423, DOI: 10.1016/s0960-9822(00)00446-2.Peer-Reviewed Original ResearchConceptsClathrin adaptor AP-2Adaptor AP-2AP-2Synaptojanin 1Unique carboxy-terminal regionClathrin coat dynamicsAlpha-adaptin subunitCarboxy-terminal domainCarboxy-terminal extensionAmino-terminal domainSynaptic vesicle recyclingCarboxy-terminal regionBinding of clathrinReceptor-mediated endocytosisChinese hamster ovary cellsActin functionPolyphosphoinositide phosphataseEar domainClathrin coatHamster ovary cellsVesicle recyclingVariety of tissuesTransferrin uptakePleiotropic rolesClathrin
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 surfaceProteinThe 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 siteSynaptotagminClathrinMotifProteinRecruitmentMembraneEndocytosisTyrosineBindingCellsPeptidesFunctional 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
1998
Endocytosis 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 linkClathrinEndocytosisGenesAdaptorBiologyMutationsRearrangementCancerTargetGeneration 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
1997
Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15
Haffner C, Takei K, Chen H, Ringstad N, Hudson A, Butler M, Salcini A, Di Fiore P, De Camilli P. Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15. FEBS Letters 1997, 419: 175-180. PMID: 9428629, DOI: 10.1016/s0014-5793(97)01451-8.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCalcium-Binding ProteinsClathrinEndocytosisHumansImmunohistochemistryIntracellular Signaling Peptides and ProteinsMolecular Sequence DataNerve EndingsNerve Tissue ProteinsPhosphoproteinsPhosphoric Monoester HydrolasesRatsSequence AlignmentSynaptic TransmissionSynaptic VesiclesConceptsSynaptojanin 1Endocytic intermediatesClathrin-coated pitsCOOH-terminal regionEH domainSpecies threeEps15Multiplicity of interactionsPutative roleClathrinNerve terminalsEndocytosisIsoformsProteinPrevious dataMotifInositolIntermediatesBindingInteractionPhenylalanineLocalizationNew evidenceDomain
1995
The function of dynamin in endocytosis
De Camilli P, Takei K, McPherson P. The function of dynamin in endocytosis. Current Opinion In Neurobiology 1995, 5: 559-565. PMID: 8580706, DOI: 10.1016/0959-4388(95)80059-x.Peer-Reviewed Original ResearchConceptsFunction of dynaminSynaptic vesicle endocytosisShibire geneShibire mutantsGTPase dynaminDrosophila melanogasterVesicle endocytosisVesicle fissionRestrictive temperatureGTP hydrolysisConformational changesDynaminEssential roleEndocytosisForm ringsRecent studiesMelanogasterClathrinMutantsGenesFissionHydrolysis