2018
A liquid phase of synapsin and lipid vesicles
Milovanovic D, Wu Y, Bian X, De Camilli P. A liquid phase of synapsin and lipid vesicles. Science 2018, 361: 604-607. PMID: 29976799, PMCID: PMC6191856, DOI: 10.1126/science.aat5671.Peer-Reviewed Original ResearchConceptsSynaptic vesiclesNeurotransmitter-containing synaptic vesiclesCalmodulin-dependent protein kinase IILipid vesiclesCalcium/calmodulin-dependent protein kinase IIProtein kinase IISmall lipid vesiclesKinase IILiquid-liquid phase separationSynapsinDistinct liquid phasesVesiclesTight clusterSynapsin 1Presynaptic sitesPhosphorylationExocytosis
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 ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsBrainCarrier ProteinsProtein BindingProtein IsoformsRatsSrc Homology DomainsSynapsesConceptsEndophilin-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 members
2000
Specificity of the Binding of Synapsin I to Src Homology 3 Domains*
Onofri F, Giovedı̀ S, Kao H, Valtorta F, Borbone L, De Camilli P, Greengard P, Benfenati F. Specificity of the Binding of Synapsin I to Src Homology 3 Domains*. Journal Of Biological Chemistry 2000, 275: 29857-29867. PMID: 10899172, DOI: 10.1074/jbc.m006018200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleProtein BindingRabbitsSignal TransductionSrc Homology DomainsSubstrate SpecificitySynapsinsConceptsSrc homology 3 domainSH3 domainCOOH-terminal regionSynapsin ISignal transductionC-SrcSynaptic vesicle-associated phosphoproteinsMultiple SH3 domainsGTPase-activating proteinsProtein-protein interactionsMitogen-activated protein kinaseDependent protein kinase IIProtein kinase IICytoskeleton assemblyP85 subunitDistinct binding patternsHigh-affinity interactionProtein kinaseAmphiphysin IC gammaKinase IIAlpha-spectrinGrb2SH3Synaptic vesiclesFission and Uncoating of Synaptic Clathrin-Coated Vesicles Are Perturbed by Disruption of Interactions with the SH3 Domain of Endophilin
Gad H, Ringstad N, Löw P, Kjaerulff O, Gustafsson J, Wenk M, Di Paolo G, Nemoto Y, Crum J, Ellisman M, De Camilli P, Shupliakov O, Brodin L. Fission and Uncoating of Synaptic Clathrin-Coated Vesicles Are Perturbed by Disruption of Interactions with the SH3 Domain of Endophilin. Neuron 2000, 27: 301-312. PMID: 10985350, DOI: 10.1016/s0896-6273(00)00038-6.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsBinding, CompetitiveCarrier ProteinsClathrinCloning, MolecularCoated Pits, Cell-MembraneDynaminsGTP PhosphohydrolasesLampreysMicroinjectionsMolecular Sequence DataNerve Tissue ProteinsPeptide FragmentsPhosphoric Monoester HydrolasesSequence Homology, Amino AcidSrc Homology DomainsSynaptic VesiclesConceptsProline-rich domainSynaptic vesicle endocytosisSH3 domainVesicle endocytosisEndophilin's SH3 domainClathrin coat formationClathrin-coated vesiclesClathrin-coated pitsDisruption of interactionsEndocytic intermediatesProteinprotein interactionsCoat formationEndophilinMolecular switchUncoatingEndocytosisVesicles
1999
Endophilin/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 stagesCoatMachineryInvagination
1998
Role of Phosphorylation in Regulation of the Assembly of Endocytic Coat Complexes
Slepnev V, Ochoa G, Butler M, Grabs D, De Camilli P. Role of Phosphorylation in Regulation of the Assembly of Endocytic Coat Complexes. Science 1998, 281: 821-824. PMID: 9694653, DOI: 10.1126/science.281.5378.821.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Protein Complex beta SubunitsAdaptor Proteins, Vesicular TransportAdenosine TriphosphateAnimalsBinding SitesCarbazolesChromatography, AffinityClathrinCyclosporineDimerizationDynamin IDynaminsEndocytosisEnzyme InhibitorsGTP PhosphohydrolasesIndole AlkaloidsMembrane ProteinsNerve Tissue ProteinsPhosphoric Monoester HydrolasesRatsRecombinant Fusion ProteinsSrc Homology DomainsPerturbation of Dynamin II with an Amphiphysin SH3 Domain Increases GLUT4 Glucose Transporters at the Plasma Membrane in 3T3-L1 Adipocytes DYNAMIN II PARTICIPATES IN GLUT4 ENDOCYTOSIS*
Volchuk A, Narine S, Foster L, Grabs D, De Camilli P, Klip A. Perturbation of Dynamin II with an Amphiphysin SH3 Domain Increases GLUT4 Glucose Transporters at the Plasma Membrane in 3T3-L1 Adipocytes DYNAMIN II PARTICIPATES IN GLUT4 ENDOCYTOSIS*. Journal Of Biological Chemistry 1998, 273: 8169-8176. PMID: 9525921, DOI: 10.1074/jbc.273.14.8169.Peer-Reviewed Original ResearchConceptsGLUT4 endocytosisDynamin IIGLUT4 glucose transportersPlasma membraneCell surfaceSH3 domainClathrin-coated vesicle formationFusion proteinGlucose transporterLevels of GLUT4Amphiphysin SH3 domainLow-density microsomal fractionIsolated plasma membranesTransferrin endocytosisEndocytic systemGLUT4 internalizationProtein dynaminGlutathione S-transferaseEndosomal compartmentsGLUT4 distributionVesicle formationDynamin peptideEndocytosisGLUT4S-transferase
1997
Synapsin I interacts with c-Src and stimulates its tyrosine kinase activity
Onofri F, Giovedì S, Vaccaro P, Czernik A, Valtorta F, De Camilli P, Greengard P, Benfenati F. Synapsin I interacts with c-Src and stimulates its tyrosine kinase activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 12168-12173. PMID: 9342381, PMCID: PMC23739, DOI: 10.1073/pnas.94.22.12168.Peer-Reviewed Original ResearchConceptsTyrosine kinase activityC-SrcKinase activitySynapsin ISrc homology 3 domainNonreceptor tyrosine kinase c-SrcSynaptic vesicle-associated phosphoproteinsTyrosine kinase c-SrcSynaptic vesiclesC-Src SH3 domainKinase c-SrcEndogenous tyrosine kinase activityTotal cellular poolStoichiometric phosphorylationSynaptic vesicle preparationsCoprecipitation assaysSignal transductionProtein speciesCellular poolRegulatory sitesBinding proteinVesicle preparationsDetergent extractsSeveralfold stimulationAffinity chromatographyThe SH3p4/Sh3p8/SH3p13 protein family: Binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain
Ringstad N, Nemoto Y, De Camilli P. The SH3p4/Sh3p8/SH3p13 protein family: Binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 8569-8574. PMID: 9238017, PMCID: PMC23017, DOI: 10.1073/pnas.94.16.8569.Peer-Reviewed Original ResearchConceptsSrc homology 3 domainSynaptic vesicle recyclingDynamin IProtein familyVesicle recyclingSH3 domain-containing proteinsDomain-containing proteinsProline-rich domainTwo-hybrid methodPhysiological binding partnerProline-rich tailRat brain libraryFurther biochemical studiesSH3 domainSynaptojaninDynamin I.Nerve terminal proteinBinding partnerTerminal proteinAmphiphysin IRelated proteinsBrain libraryMultiple tissuesBiochemical studiesProteinAmphiphysin II (SH3P9; BIN1), a Member of the Amphiphysin/Rvs Family, Is Concentrated in the Cortical Cytomatrix of Axon Initial Segments and Nodes of Ranvier in Brain and around T Tubules in Skeletal Muscle
Butler M, David C, Ochoa G, Freyberg Z, Daniell L, Grabs D, Cremona O, De Camilli P. Amphiphysin II (SH3P9; BIN1), a Member of the Amphiphysin/Rvs Family, Is Concentrated in the Cortical Cytomatrix of Axon Initial Segments and Nodes of Ranvier in Brain and around T Tubules in Skeletal Muscle. Journal Of Cell Biology 1997, 137: 1355-1367. PMID: 9182667, PMCID: PMC2132527, DOI: 10.1083/jcb.137.6.1355.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsAxonsBase SequenceBrain ChemistryCarrier ProteinsCerebral CortexCloning, MolecularCOS CellsCytoplasmDNA, ComplementaryGene ExpressionHumansMiceMolecular Sequence DataMuscle ProteinsMuscle, SkeletalNerve Tissue ProteinsNuclear ProteinsRabbitsRanvier's NodesRatsSrc Homology DomainsTumor Cells, CulturedTumor Suppressor ProteinsConceptsAmphiphysin IICortical cytoplasmPresence of clathrinSkeletal muscleParaneoplastic stiff-man syndromeAxon initial segmentYeast homologueActin functionNuclear functionsActin cytoskeletonActin dynamicsMammalian cellsActin cytomatrixPleiotropic functionsDistinct domainsNeuronal proteinsSplice variantsT-tubulesAmphiphysinCytomatrixEndocytosisPutative roleNodes of RanvierCytoplasmIsoformsThe 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