2001
Differential Expression of Endophilin 1 and 2 Dimers at Central Nervous System Synapses*
Ringstad N, Nemoto Y, De Camilli P. Differential Expression of Endophilin 1 and 2 Dimers at Central Nervous System Synapses*. Journal Of Biological Chemistry 2001, 276: 40424-40430. PMID: 11518713, DOI: 10.1074/jbc.m106338200.Peer-Reviewed Original ResearchConceptsEndophilin-1SH3 domain-mediated interactionsDiverse cellular proteinsDomain-mediated interactionsSynaptic vesicle biogenesisNH2-terminal moietyCoiled-coil domainCentral nervous system synapsesGTPase dynaminVesicle biogenesisDifferent cellular targetsEndocytic machineryCellular proteinsSynaptojanin 1Endophilin isoformsRelated proteinsDifferential expressionCellular targetsStable dimerSynaptojaninDynaminSame complexProteinCentral synapsesFamily membersThe 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
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)
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 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 processesClathrinSynaptotagminComplexesExocytosisCalcineurinMachineryProteinEpidermal 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 geneGenesProliferation