1999
The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein Module*
Rosenthal J, Chen H, Slepnev V, Pellegrini L, Salcini A, Di Fiore P, De Camilli P. The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein Module*. Journal Of Biological Chemistry 1999, 274: 33959-33965. PMID: 10567358, DOI: 10.1074/jbc.274.48.33959.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsCalcium-Binding ProteinsCarrier ProteinsCHO CellsClathrinCoated VesiclesCricetinaeDNA, ComplementaryFluorescent Antibody TechniqueGene ExpressionHumansIntracellular Signaling Peptides and ProteinsLuciferasesMaleMembrane ProteinsMolecular Sequence DataNeuropeptidesPhosphoproteinsPhylogenyProtein BindingProtein Structure, TertiaryRatsRecombinant Fusion ProteinsSequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidTissue DistributionVesicular Transport ProteinsConceptsEpsin 1Clathrin coatClathrin adaptor AP-2New protein modulesNew protein familyTerminal regionAdaptor AP-2Family of proteinsRat brain libraryNPF motifsProtein modulesProtein familyCell peripheryAP-2Membrane dynamicsSimilar proteinsBrain libraryClathrinEps15Vesicle fractionEpsinGreen fluorescentGolgi regionCell surfaceProtein
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 analysisSeb1A 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
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 levels