2001
Identification and Characterization of a Synaptojanin 2 Splice Isoform Predominantly Expressed in Nerve Terminals*
Nemoto Y, Wenk M, Watanabe M, Daniell L, Murakami T, Ringstad N, Yamada H, Takei K, De Camilli P. Identification and Characterization of a Synaptojanin 2 Splice Isoform Predominantly Expressed in Nerve Terminals*. Journal Of Biological Chemistry 2001, 276: 41133-41142. PMID: 11498538, DOI: 10.1074/jbc.m106404200.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBase SequenceChromatography, AffinityCloning, MolecularDNA PrimersGTP PhosphohydrolasesHumansMolecular Sequence DataMutagenesis, Site-DirectedNerve EndingsNerve Tissue ProteinsPhosphoric Monoester HydrolasesProtein IsoformsRac1 GTP-Binding ProteinRatsRNA SplicingSequence Homology, Amino Acid
2000
Functional Characterization of a Mammalian Sac1 and Mutants Exhibiting Substrate-specific Defects in Phosphoinositide Phosphatase Activity*
Nemoto Y, Kearns B, Wenk M, Chen H, Mori K, Alb J, De Camilli P, Bankaitis V. Functional Characterization of a Mammalian Sac1 and Mutants Exhibiting Substrate-specific Defects in Phosphoinositide Phosphatase Activity*. Journal Of Biological Chemistry 2000, 275: 34293-34305. PMID: 10887188, DOI: 10.1074/jbc.m003923200.Peer-Reviewed Original ResearchConceptsSubstrate-specific defectsIntegral membrane proteinsPhosphoinositide phosphatase activityPhosphatase activityMembrane proteinsEndoplasmic reticulumGolgi secretory functionIntegral membrane lipidEukaryotic cell physiologyPrimary sequence homologyYeast Sac1pSAC1 geneHeterologous complementationActin functionSac1 domainSac1pBisphosphate substrateMembrane phosphoinositidesPhosphatidylinositol 3Cell physiologyFunctional characterizationGene productsSequence homologyProtein activityGolgi complex
1999
Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein
Nemoto Y, De Camilli P. Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein. The EMBO Journal 1999, 18: 2991-3006. PMID: 10357812, PMCID: PMC1171381, DOI: 10.1093/emboj/18.11.2991.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsBase SequenceBinding SitesCarrier ProteinsCHO CellsCloning, MolecularCricetinaeCytoplasmExonsIntracellular MembranesIsoenzymesMembrane ProteinsMitochondriaMolecular Sequence DataMutationNerve Tissue ProteinsPhosphoric Monoester HydrolasesProtein BindingRatsRecombinant Fusion ProteinsRNA, MessengerYeastsConceptsMitochondrial outer membrane proteinMitochondrial outer membraneOuter membrane proteinsPDZ domainMembrane proteinsSynaptojanin 2Outer membraneNovel mitochondrial outer membrane proteinC-terminal transmembrane regionSingle PDZ domainPerinuclear clusteringTransmembrane regionSynaptojanin 1C-terminusExon sequencesSpliced formsEnforced expressionUnique motifModulation of inositolIntracellular distributionSynaptic vesiclesMitochondriaPutative roleOmp25ProteinThe Interaction of Epsin and Eps15 with the Clathrin Adaptor AP-2 Is Inhibited by Mitotic Phosphorylation and Enhanced by Stimulation-dependent Dephosphorylation in Nerve Terminals*
Chen H, Slepnev V, Di Fiore P, De Camilli P. The Interaction of Epsin and Eps15 with the Clathrin Adaptor AP-2 Is Inhibited by Mitotic Phosphorylation and Enhanced by Stimulation-dependent Dephosphorylation in Nerve Terminals*. Journal Of Biological Chemistry 1999, 274: 3257-3260. PMID: 9920862, DOI: 10.1074/jbc.274.6.3257.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsBase SequenceCalcium-Binding ProteinsCarrier ProteinsCell LineDNA PrimersEndocytosisExocytosisIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceMitosisNerve EndingsNeuropeptidesPhosphoproteinsPhosphorylationProtein BindingRatsVesicular Transport Proteins
1997
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
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 RanvierCytoplasmIsoforms
1996
Yeast protein translocation complex: Isolation of two genes SEB1 and SEB2 encoding proteins homologous to the Sec61β subunit
Toikkanen J, Gatti E, Takei K, Saloheimo M, Olkkonen V, Söderlund H, De Camilli P, Keränen S. Yeast protein translocation complex: Isolation of two genes SEB1 and SEB2 encoding proteins homologous to the Sec61β subunit. Yeast 1996, 12: 425-438. PMID: 8740416, DOI: 10.1002/(sici)1097-0061(199604)12:5<425::aid-yea924>3.0.co;2-b.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBiological TransportCell LineChlorocebus aethiopsCloning, MolecularCytoplasmDNA, ComplementaryDogsEndoplasmic ReticulumFungal ProteinsGenes, FungalGenes, SuppressorMembrane ProteinsMembrane Transport ProteinsMicrosomesMolecular Sequence DataMolecular WeightSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSEC Translocation ChannelsSequence Analysis, DNASequence Homology, Amino AcidVesicular Transport ProteinsConceptsBeta subunitN-terminal signal sequencePotential membrane-spanning regionsEndoplasmic reticulumProtein translocation apparatusMembrane-spanning regionNovel genetic toolsTemperature-sensitive phenotypeHydrophilic N-terminusEvolutionary conservationTranslocation apparatusYeast genesHeterologous hybridizationProtein translocationHomologous genesER membraneGenetic toolsSignal sequenceChromosomal disruptionMulticopy plasmidC-terminusDouble disruptionN-terminusFunctional analysisSeb1
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 levelsAutoimmunity 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
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
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