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
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 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 surfaceProtein
1995
Targeting of the 67-kDa Isoform of Glutamic Acid Decarboxylase to Intracellular Organelles Is Mediated by Its Interaction with the NH2-terminal Region of the 65-kDa Isoform of Glutamic Acid Decarboxylase (∗)
Dirkx R, Thomas A, Li L, Lernmark Å, Sherwin R, De Camilli P, Solimena M. Targeting of the 67-kDa Isoform of Glutamic Acid Decarboxylase to Intracellular Organelles Is Mediated by Its Interaction with the NH2-terminal Region of the 65-kDa Isoform of Glutamic Acid Decarboxylase (∗). Journal Of Biological Chemistry 1995, 270: 2241-2246. PMID: 7836456, DOI: 10.1074/jbc.270.5.2241.Peer-Reviewed Original ResearchConceptsGolgi complex regionNH2-terminal regionGlutamic acid decarboxylaseAbsence of palmitoylationSoluble cytosolic proteinsAcid decarboxylaseRegions of GAD65Cytosolic proteinsNeurotransmitter gamma-aminobutyric acidDetergent phasePerinuclear regionExtracts of brainIntracellular distributionGamma-aminobutyric acidPellet fractionComplex regionIsoformsProteinFibroblastsGAD67GAD65DecarboxylaseTriton XPalmitoylationNeurons
1994
Synaptic targeting of rabphilin-3A, a synaptic vesicle Ca2+/phospholipid-binding protein, depends on rab3A/3C
Li C, Takei K, Geppert M, Daniell L, Stenius K, Chapman E, Jahn R, De Camilli P, Südhof T. Synaptic targeting of rabphilin-3A, a synaptic vesicle Ca2+/phospholipid-binding protein, depends on rab3A/3C. Neuron 1994, 13: 885-898. PMID: 7946335, DOI: 10.1016/0896-6273(94)90254-2.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsBase SequenceBiological EvolutionBrain ChemistryConserved SequenceDNA, ComplementaryFluorescent Antibody TechniqueGlutathione TransferaseGTP-Binding ProteinsMiceMice, Mutant StrainsMicroscopy, ImmunoelectronMolecular Sequence DataNerve Tissue ProteinsNeuronsRab GTP-Binding ProteinsRab3 GTP-Binding ProteinsRatsRecombinant Fusion ProteinsVesicular Transport ProteinsConceptsGTP-dependent mannerSynaptic vesicle membraneRabphilin-3AVesicle membraneLow molecular weight GTPPeripheral membrane proteinsSynaptic vesiclesSynaptic vesicle dockingRab3A-deficient miceSynaptic vesicle proteinsMembrane recruitmentVesicle dockingPutative functionsMembrane proteinsWeight GTPVesicle proteinsN-terminusSynaptic targetingRab3CRab3AProteinVesiclesMembraneSynaptic patternsNormal levels
1990
Substance P-like immunoreactivity at the frog neuromuscular junction
Matteoli M, Haimann C, De Camilli P. Substance P-like immunoreactivity at the frog neuromuscular junction. Neuroscience 1990, 37: 271-275. PMID: 1700842, DOI: 10.1016/0306-4522(90)90213-n.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAnimalsCalcitonin Gene-Related PeptideFluorescent Antibody TechniqueMotor NeuronsNerve EndingsNeuromuscular JunctionRana pipiensReceptors, NicotinicSpinal CordSubstance PConceptsLike immunoreactivitySubstance PNerve terminalsCalcitonin gene-related peptide-like immunoreactivityGene-related peptide-like immunoreactivityFrog motor nerve endingsPeptide-like immunoreactivityMotor nerve endingsLarge dense-core vesiclesFrog neuromuscular junctionDense-core vesiclesCholinergic transmissionNerve endingsSame neuronsNeuromuscular junctionImmunoreactivityFrog motoneuronsPhysiological roleImmunofluorescence approachPrevious dataMotoneuronsNeurons
1989
Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor
Mignery G, Südhof T, Takei K, De Camilli P. Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor. Nature 1989, 342: 192-195. PMID: 2554146, DOI: 10.1038/342192a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium ChannelsCerebellumCloning, MolecularFluorescent Antibody TechniqueImmunohistochemistryInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsIntracellular MembranesMiceMolecular Sequence DataPurkinje CellsReceptors, Cell SurfaceReceptors, CholinergicReceptors, Cytoplasmic and NuclearRyanodineRyanodine Receptor Calcium Release ChannelConceptsEndoplasmic reticulumCalcium channel proteinsIntracellular second messengerRelative molecular massIntracellular membranesSecond messengerIntracellular compartmentsMolecular massEfficacy of neurotransmissionPutative receptorDirect roleProteinCalcium releaseGrowth factorReticulumDendritic spinesTrisphosphateIntracellular storesPresynaptic terminalsInositolIntracellular calcium storesReceptorsCalcium storesRNA6Immunocytochemistry
1986
Demonstration and localization of synapsin I in vestibular receptors in the cat: immunocytochemical study.
Scarfone E, Favre D, De Camilli P, Sans A. Demonstration and localization of synapsin I in vestibular receptors in the cat: immunocytochemical study. Comptes Rendus Biologies 1986, 302: 567-72. PMID: 3091199.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCatsEpithelial CellsFluorescent Antibody TechniqueImmune SeraImmunoenzyme TechniquesNerve Tissue ProteinsSensory Receptor CellsSynapsinsVestibule, LabyrinthConceptsNerve chaliceSynapsin IType I hair cellsType II hair cellsHair cellsEfferent nerve endingsSynaptic vesiclesI hair cellsPeroxidase-antiperoxidase techniqueNumerous synaptic vesiclesAxodendritic synapsesVestibular receptorsAxosomatic synapsesNerve endingsSmall synaptic vesiclesSynaptic endingsPAP stainingVestibular epitheliaStrong immunoreactivitySensory endingsImmunocytochemical studyNeuron-specific phosphoproteinImmunoreactivityEpitheliumSynapses