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 proteinsProteinAn Evolutionarily Conserved Domain in a Subfamily of Rabs Is Crucial for the Interaction with the Guanyl Nucleotide Exchange Factor Mss4*
Burton J, Slepnev V, De Camilli P. An Evolutionarily Conserved Domain in a Subfamily of Rabs Is Crucial for the Interaction with the Guanyl Nucleotide Exchange Factor Mss4*. Journal Of Biological Chemistry 1997, 272: 3663-3668. PMID: 9013620, DOI: 10.1074/jbc.272.6.3663.Peer-Reviewed Original Research
1996
Alzheimer Amyloid Protein Precursor Is Localized in Nerve Terminal Preparations to Rab5-containing Vesicular Organelles Distinct from Those Implicated in the Synaptic Vesicle Pathway*
Ikin A, Annaert W, Takei K, De Camilli P, Jahn R, Greengard P, Buxbaum J. Alzheimer Amyloid Protein Precursor Is Localized in Nerve Terminal Preparations to Rab5-containing Vesicular Organelles Distinct from Those Implicated in the Synaptic Vesicle Pathway*. Journal Of Biological Chemistry 1996, 271: 31783-31786. PMID: 8943215, DOI: 10.1074/jbc.271.50.31783.Peer-Reviewed Original ResearchConceptsAmyloid protein precursorSmall synaptic vesiclesSynaptic vesiclesVesicular organellesProtein precursorSynaptic vesicle recycling pathwayNerve terminal preparationsSynaptic vesicle pathwayVesicle recycling pathwayAlzheimer amyloid protein precursorRecycling pathwayVesicle pathwayOrganellesVesiclesImmunoisolatesPathwayHomogeneous populationRab5Nerve terminalsHigh levelsDistinctPrecursorsSubstantial numberBilamellar vesicles
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 levelsThe 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
1993
A mammalian guanine-nucleotide-releasing protein enhances function of yeast secretory protein Sec4
Burton J, Roberts D, Montaldi M, Novick P, Camilli P. A mammalian guanine-nucleotide-releasing protein enhances function of yeast secretory protein Sec4. Nature 1993, 361: 464-467. PMID: 8429887, DOI: 10.1038/361464a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsATP-Binding Cassette TransportersBase SequenceBlotting, NorthernBrain ChemistryCarrier ProteinsCloning, MolecularDNAEscherichia coliEscherichia coli ProteinsGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsGuanosine DiphosphateGuanosine TriphosphateMaltose-Binding ProteinsMolecular Sequence DataMonosaccharide Transport ProteinsPhosphotransferasesPhosphotransferases (Alcohol Group Acceptor)ProteinsRab GTP-Binding ProteinsRatsRecombinant Fusion ProteinsRecombinant ProteinsRestriction MappingRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidConceptsYeast secretory proteinsGTP-GDP cycleHydrolysis of GTPSimilar biochemical propertiesMammalian guanineMss4 proteinYeast proteinsSmall GTPSecretory pathwaySequence similarityAccessory proteinsProtein Rab3AGDP releaseSecretory proteinsMolecular switchComplementary DNABiochemical propertiesGTPMss4ProteinEnhance functionDifferent conformationsYeast6RAS2DSS4