2001
The 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
2000
Dual interaction of synaptotagmin with μ2‐ and α‐adaptin facilitates clathrin‐coated pit nucleation
Haucke V, Wenk M, Chapman E, Farsad K, De Camilli P. Dual interaction of synaptotagmin with μ2‐ and α‐adaptin facilitates clathrin‐coated pit nucleation. The EMBO Journal 2000, 19: 6011-6019. PMID: 11080148, PMCID: PMC305843, DOI: 10.1093/emboj/19.22.6011.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex 1Adaptor Protein Complex 2Adaptor Protein Complex 3Adaptor Protein Complex alpha SubunitsAdaptor Protein Complex mu SubunitsAdaptor Proteins, Vesicular TransportAnimalsBinding SitesCalcium-Binding ProteinsCHO CellsClathrinCoated Pits, Cell-MembraneCricetinaeIn Vitro TechniquesLiposomesLysineMembrane GlycoproteinsMembrane ProteinsMutationNerve Tissue ProteinsPhosphoproteinsProtein SubunitsRatsSynaptic VesiclesSynaptotagminsTyrosineConceptsAP-2C2B domainEndocytic adaptor complex AP-2Endocytic clathrin-coated pitsAdaptor complex AP-2Clathrin adaptor AP-2Synaptic vesicle protein synaptotagminTyrosine-based sorting motifAdaptor AP-2Clathrin-coated pitsMajor docking siteKey physiological rolesDual interactionSorting motifClathrin coatTransferrin internalizationProtein synaptotagminDocking siteSubdomain BSynaptotagminPhysiological roleLiving cellsSynaptic vesiclesSubunitsMu2Epsin 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 surfaceProteinEpidermal 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
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
1989
Synapsins: Mosaics of Shared and Individual Domains in a Family of Synaptic Vesicle Phosphoproteins
Südhof T, Czernik A, Kao H, Takei K, Johnston P, Horiuchi A, Kanazir S, Wagner M, Perin M, De Camilli P, Greengard P. Synapsins: Mosaics of Shared and Individual Domains in a Family of Synaptic Vesicle Phosphoproteins. Science 1989, 245: 1474-1480. PMID: 2506642, DOI: 10.1126/science.2506642.Peer-Reviewed Original ResearchConceptsDistinct signal transduction pathwaysHomologous amino-terminal domainsAmino-terminal domainCarboxyl-terminal domainSignal transduction pathwaysNeurotransmitter releaseDifferential splicingMolecular cloningTransduction pathwaysSynaptic vesicle phosphoproteinsHomologous proteinsNeuronal phosphoproteinSynaptic vesiclesMessenger RNASynapsinStructural diversityIndividual domainsPhosphoproteinDifferential distributionTypes of neuronsRelative amountsDomainSplicingCytoskeletonDifferent roles