2022
Multimodal imaging of synaptic vesicles with a single probe
An SJ, Stagi M, Gould TJ, Wu Y, Mlodzianoski M, Rivera-Molina F, Toomre D, Strittmatter SM, De Camilli P, Bewersdorf J, Zenisek D. Multimodal imaging of synaptic vesicles with a single probe. Cell Reports Methods 2022, 2: 100199. PMID: 35497490, PMCID: PMC9046237, DOI: 10.1016/j.crmeth.2022.100199.Peer-Reviewed Original ResearchConceptsC2 domainSynaptic vesiclesSynaptic vesicle recyclingMembrane-binding C2 domainMultiple microscopy methodsEndocytic markersMembrane recyclingVesicle functionVesicle populationsCytosolic phospholipase ACell typesPhospholipase ADetectable tagMicroscopy modalitiesModular probesMultiple microscopy techniquesVesiclesComplete understandingDomainMicroscopy methodsMultiple levelsProbeAvailable probesMicroscopy techniquesPathway
2009
Mechanistic Insights into Membrane Remodeling Through BAR‐Domain Proteins
Frost A, Mim C, Perera R, Spasov K, Egelman E, De Camilli P, Unger V. Mechanistic Insights into Membrane Remodeling Through BAR‐Domain Proteins. The FASEB Journal 2009, 23: 82.2-82.2. DOI: 10.1096/fasebj.23.1_supplement.82.2.Peer-Reviewed Original ResearchF-BAR domainBAR domain proteinsMembrane-bound stateDifferent molecular surfacesMembrane remodelingCellular physiologyMembrane curvatureElectron cryomicroscopyMechanistic insightsCooperative assemblyConstituent membranesProteinStructural informationMolecular surfaceFunctional stateMembraneDomainSubtle changesCryomicroscopyBilayer substratePhysiologyStructural modelAssemblyRemodelingCells
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
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 evidenceDomainThe SH3 Domain of Amphiphysin Binds the Proline-rich Domain of Dynamin at a Single Site That Defines a New SH3 Binding Consensus Sequence*
Grabs D, Slepnev V, Songyang Z, David C, Lynch M, Cantley L, De Camilli P. The SH3 Domain of Amphiphysin Binds the Proline-rich Domain of Dynamin at a Single Site That Defines a New SH3 Binding Consensus Sequence*. Journal Of Biological Chemistry 1997, 272: 13419-13425. PMID: 9148966, DOI: 10.1074/jbc.272.20.13419.Peer-Reviewed Original ResearchConceptsSH3 domainDynamin ILong proline-rich regionProline-rich domainSynaptic vesicle endocytosisProline-rich regionPeptide library approachMultiple SH3Adjacent amino acidsVesicle endocytosisCombinatorial peptide library approachConsensus sequenceAmphiphysinNeuronal proteinsSingle siteAmino acidsSH3Library approachProteinHigh affinityDomainDynaminGTPaseSitesEndocytosisSynaptic 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
1996
A presynaptic inositol-5-phosphatase
McPherson P, Garcia E, Slepnev V, David C, Zhang X, Grabs D, Sossini W, Bauerfeind R, Nemoto Y, De Camilli P. A presynaptic inositol-5-phosphatase. Nature 1996, 379: 353-357. PMID: 8552192, DOI: 10.1038/379353a0.Peer-Reviewed Original ResearchConceptsSH3 domainAmino-terminal domainSynaptic vesicle recyclingRelative molecular massPutative functionsNerve terminal proteinSynaptojaninTerminal proteinVesicle recyclingMajor brain proteinsCarboxy terminusTermination sitesMolecular massOculocerebrorenal syndromeSynaptic vesiclesPresynaptic proteinsDynaminPhosphoinositide metabolismProteinBrain proteinsPhospholipid metabolismMetabolismGrb2DomainGenes
1994
Autoimmunity in Stiff‐Man Syndrome with breast cancer is targeted to the C‐terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161
David C, Solimena M, De Camilli P. Autoimmunity in Stiff‐Man Syndrome with breast cancer is targeted to the C‐terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161. FEBS Letters 1994, 351: 73-79. PMID: 8076697, DOI: 10.1016/0014-5793(94)00826-4.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAutoantibodiesBase SequenceBreast NeoplasmsChickensCloning, MolecularCytoskeletal ProteinsFungal ProteinsHumansMicrofilament ProteinsMolecular Sequence DataNerve Tissue ProteinsOligodeoxyribonucleotidesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidStiff-Person SyndromeConceptsC-terminal regionStiff-man syndromeYeast proteinsUnfavourable growth conditionsBreast cancerSH3 domainTerminal domainAmphiphysinNeuronal proteinsRvs167Rvs161ProteinCell entryPatient autoantibodiesGrowth conditionsSynaptic membranesSyndromeCancerDistinct patternsStationary phaseDomainChickensAutoantibodiesAutoimmunityAutoantigens
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