2000
Dual interaction of synaptotagmin with μ2‐ and α‐adaptin facilitates clathrin‐coated pit nucleation
Haucke V, Wenk M, Chapman E, Farsad K, De Camilli P. Dual interaction of synaptotagmin with μ2‐ and α‐adaptin facilitates clathrin‐coated pit nucleation. The EMBO Journal 2000, 19: 6011-6019. PMID: 11080148, PMCID: PMC305843, DOI: 10.1093/emboj/19.22.6011.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex 1Adaptor Protein Complex 2Adaptor Protein Complex 3Adaptor Protein Complex alpha SubunitsAdaptor Protein Complex mu SubunitsAdaptor Proteins, Vesicular TransportAnimalsBinding SitesCalcium-Binding ProteinsCHO CellsClathrinCoated Pits, Cell-MembraneCricetinaeIn Vitro TechniquesLiposomesLysineMembrane GlycoproteinsMembrane ProteinsMutationNerve Tissue ProteinsPhosphoproteinsProtein SubunitsRatsSynaptic VesiclesSynaptotagminsTyrosineConceptsAP-2C2B domainEndocytic adaptor complex AP-2Endocytic clathrin-coated pitsAdaptor complex AP-2Clathrin adaptor AP-2Synaptic vesicle protein synaptotagminTyrosine-based sorting motifAdaptor AP-2Clathrin-coated pitsMajor docking siteKey physiological rolesDual interactionSorting motifClathrin coatTransferrin internalizationProtein synaptotagminDocking siteSubdomain BSynaptotagminPhysiological roleLiving cellsSynaptic vesiclesSubunitsMu2
1999
Essential Role of Phosphoinositide Metabolism in Synaptic Vesicle Recycling
Cremona O, Di Paolo G, Wenk M, Lüthi A, Kim W, Takei K, Daniell L, Nemoto Y, Shears S, Flavell R, McCormick D, De Camilli P. Essential Role of Phosphoinositide Metabolism in Synaptic Vesicle Recycling. Cell 1999, 99: 179-188. PMID: 10535736, DOI: 10.1016/s0092-8674(00)81649-9.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell-Free SystemCerebral CortexCoated Pits, Cell-MembraneEndocytosisEnzyme InhibitorsExonsHippocampusIn Vitro TechniquesMembrane PotentialsMiceMice, KnockoutMicroscopy, ElectronNerve EndingsNerve Tissue ProteinsNeuronsPhosphatidylinositolsPhosphoric Monoester HydrolasesSynaptic Vesicles
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
The role of Rab3A in neurotransmitter release
Geppert M, Bolshakov V, Siegelbaum S, Takei K, De Camilli P, Hammer R, Südhof T. The role of Rab3A in neurotransmitter release. Nature 1994, 369: 493-497. PMID: 7911226, DOI: 10.1038/369493a0.Peer-Reviewed Original ResearchConceptsRole of Rab3ASynaptic vesicle exocytosisSmall GTPRab3A geneHomologous recombinationVesicle exocytosisSynaptic vesiclesHippocampal CA1 pyramidal cellsSynaptic proteinsProteinCA1 pyramidal cellsNeurotransmitter releaseExocytosisGTPPyramidal cellsRepetitive stimulationSynaptic depressionElectrophysiological recordingsRepetitive stimuliCompensatory changesShort trainsRabphilinRab3Rab3AGenes