2000
Amphiphysin 1 Binds the Cyclin-dependent Kinase (cdk) 5 Regulatory Subunit p35 and Is Phosphorylated by cdk5 and cdc2*
Floyd S, Porro E, Slepnev V, Ochoa G, Tsai L, De Camilli P. Amphiphysin 1 Binds the Cyclin-dependent Kinase (cdk) 5 Regulatory Subunit p35 and Is Phosphorylated by cdk5 and cdc2*. Journal Of Biological Chemistry 2000, 276: 8104-8110. PMID: 11113134, DOI: 10.1074/jbc.m008932200.Peer-Reviewed Original ResearchConceptsAmphiphysin 1Kinase familyCyclin-dependent protein kinase familyCyclin-dependent kinase familyProtein kinase familySynaptic vesicle endocytosisB kinase complexNeurite outgrowthSubunit p35Cyclin-dependent kinase 5NH2-terminal regionMitotic phosphorylationYeast homologueImportant physiological roleSerine 272Vesicle endocytosisActin cytoskeletonKinase complexRegulatory subunit p35Actin dynamicsPeripheral lamellipodiaDifferentiated cellsKinase 5AmphiphysinPhysiological roleAccessory factors in clathrin-dependent synaptic vesicle endocytosis
Slepnev V, De Camilli P. Accessory factors in clathrin-dependent synaptic vesicle endocytosis. Nature Reviews Neuroscience 2000, 1: 161-172. PMID: 11257904, DOI: 10.1038/35044540.Peer-Reviewed Original ResearchConceptsAccessory factorsNumerous accessory proteinsSynaptic vesicle endocytosisClathrin-mediated endocytosisRecent structural studiesPlasma membrane componentsSynaptic vesicle recyclingInternalization of receptorsVesicle endocytosisCoat assemblyExtracellular ligandsClathrin coatMolecular detailsVesicle recyclingAccessory proteinsGenetic studiesEndocytosisMembrane componentsSurface proteinsClathrinStructural studiesProteinVesiclesInternalizationNew aspectsFission 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
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 processesClathrinSynaptotagminComplexesExocytosisCalcineurinMachineryProteinEndophilin/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
Amphiphysin I Antisense Oligonucleotides Inhibit Neurite Outgrowth in Cultured Hippocampal Neurons
Mundigl O, Ochoa G, David C, Slepnev V, Kabanov A, De Camilli P. Amphiphysin I Antisense Oligonucleotides Inhibit Neurite Outgrowth in Cultured Hippocampal Neurons. Journal Of Neuroscience 1998, 18: 93-103. PMID: 9412489, PMCID: PMC6793426, DOI: 10.1523/jneurosci.18-01-00093.1998.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCalcium-Binding ProteinsCells, CulturedDynamin IDynaminsEndocytosisGene ExpressionGTP PhosphohydrolasesHippocampusMembrane GlycoproteinsMiceNerve Tissue ProteinsNeuritesOligonucleotides, AntisensePhosphoric Monoester HydrolasesRabbitsRatsRNA, MessengerSynaptic VesiclesSynaptotagminsTubulinConceptsAmphiphysin IDynamin ICell polarityNeurite outgrowthSynaptic vesicle endocytosisPhysiological binding partnerGrowth conesClose functional linkYeast homologActin patchesActin functionVesicle endocytosisActin dynamicsProtein familyBinding partnerCell cytoskeletonAxon formationFunctional linkNeuronal differentiationWestern blot analysisCultured hippocampal neuronsHippocampal neuronsDevelopmental stagesNeuronal proteinsAmphipathic polymers
1997
Amphiphysin I Is Associated with Coated Endocytic Intermediates and Undergoes Stimulation-dependent Dephosphorylation in Nerve Terminals*
Bauerfeind R, Takei K, De Camilli P. Amphiphysin I Is Associated with Coated Endocytic Intermediates and Undergoes Stimulation-dependent Dephosphorylation in Nerve Terminals*. Journal Of Biological Chemistry 1997, 272: 30984-30992. PMID: 9388246, DOI: 10.1074/jbc.272.49.30984.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcineurinDynamin IDynaminsElectrophoresis, Polyacrylamide GelEndocytosisEnzyme InhibitorsGTP PhosphohydrolasesGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Microscopy, ElectronMicrotubulesNerve Tissue ProteinsPhospholipase DPhosphoric Monoester HydrolasesPhosphorylationPresynaptic TerminalsRatsConceptsSrc homology 3Dynamin IAmphiphysin IEndocytic intermediatesCalcineurin-dependent dephosphorylationSynaptic vesicle endocytosisSynaptic vesicle exocytosisSynaptic vesicle recyclingClathrin-coated budsBurst of exocytosisAbundant presynaptic proteinElectron microscopy immunocytochemistryHomology 3Vesicle endocytosisVesicle exocytosisConstitutive phosphorylationVesicle recyclingRapid dephosphorylationOkadaic acidPhysiological partnersDephosphorylationBinding proteinPutative rolePresynaptic proteinsProteinSynaptic vesicle endocytosis
Cremona O, De Camilli P. Synaptic vesicle endocytosis. Current Opinion In Neurobiology 1997, 7: 323-330. PMID: 9232811, DOI: 10.1016/s0959-4388(97)80059-1.Peer-Reviewed Original ResearchThe 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 architectureSH3DomainAmphiphysinRecycling of Synaptic Vesicles
Bauerfeind R, David C, Grabs D, McPherson P, Nemoto Y, Slepnev V, Takei K, De Camilli P. Recycling of Synaptic Vesicles. Advances In Pharmacology 1997, 42: 253-257. PMID: 9327892, DOI: 10.1016/s1054-3589(08)60741-3.Peer-Reviewed Original ResearchConceptsSynaptic vesicle endocytosisSynaptic vesicle recyclingVesicle endocytosisVesicle recyclingSynaptic vesiclesPlasma membraneClathrin adaptor complex AP2Vesicular transport stepsClathrin-coated vesiclesClathrin-coated pitsMicrotubule-binding proteinSynaptic vesicle cycleRole of proteinsCell surface receptorsRole of lipidsClathrin coatRestrictive temperatureEarly endosomesGuanosine triphosphataseRecycling pathwayVesicle cycleDynaminTransport stepsEndocytosisSurface receptors
1995
The function of dynamin in endocytosis
De Camilli P, Takei K, McPherson P. The function of dynamin in endocytosis. Current Opinion In Neurobiology 1995, 5: 559-565. PMID: 8580706, DOI: 10.1016/0959-4388(95)80059-x.Peer-Reviewed Original ResearchConceptsFunction of dynaminSynaptic vesicle endocytosisShibire geneShibire mutantsGTPase dynaminDrosophila melanogasterVesicle endocytosisVesicle fissionRestrictive temperatureGTP hydrolysisConformational changesDynaminEssential roleEndocytosisForm ringsRecent studiesMelanogasterClathrinMutantsGenesFissionHydrolysis