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 roleDual 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 vesiclesSubunitsMu2Functional 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 complexTandem Arrangement of the Clathrin and AP-2 Binding Domains in Amphiphysin 1 and Disruption of Clathrin Coat Function by Amphiphysin Fragments Comprising These Sites*
Slepnev V, Ochoa G, Butler M, De Camilli P. Tandem Arrangement of the Clathrin and AP-2 Binding Domains in Amphiphysin 1 and Disruption of Clathrin Coat Function by Amphiphysin Fragments Comprising These Sites*. Journal Of Biological Chemistry 2000, 275: 17583-17589. PMID: 10748223, DOI: 10.1074/jbc.m910430199.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsBinding SitesBinding, CompetitiveCHO CellsClathrinCricetinaeGlutathione TransferaseHumansMembrane ProteinsMolecular Sequence DataMonomeric Clathrin Assembly ProteinsMutagenesis, Site-DirectedNerve Tissue ProteinsPeptide FragmentsRecombinant Fusion ProteinsTransfectionConceptsAP-2Amphiphysin 1Coat proteinClathrin adaptor AP-2COOH-terminal SH3 domainAdaptor AP-2Chinese hamster ovary cellsCoat functionMultifunctional adaptorSH3 domainHamster ovary cellsTerminal domainBinding domainsClathrinDynaminMembrane lipidsAmphiphysinSynaptic vesiclesAmino acidsSynaptojaninOvary cellsDirect interactionProteinTertiary complexTandem arrangementAutoimmunity to Gephyrin in Stiff-Man Syndrome
Butler M, Hayashi A, Ohkoshi N, Villmann C, Becker C, Feng G, De Camilli P, Solimena M. Autoimmunity to Gephyrin in Stiff-Man Syndrome. Neuron 2000, 26: 307-312. PMID: 10839351, DOI: 10.1016/s0896-6273(00)81165-4.Peer-Reviewed Original ResearchConceptsStiff-man syndromeGlutamic acid decarboxylaseCentral nervous systemInhibitory synapsesEnzyme glutamic acid decarboxylaseHigh-titer autoantibodiesSubset of casesParaneoplastic originClinical featuresSynaptic antigensMediastinal cancerNeurological conditionsRare diseaseGlycine receptorsNervous systemAcid decarboxylaseAutoimmunityPostsynaptic membraneGephyrinSpasmSyndromeSynapsesAutoantibodiesPatientsGABADirect interaction of the 170 kDa isoform of synaptojanin 1 with clathrin and with the clathrin adaptor AP-2
Haffner C, Di Paolo G, Rosenthal J, De Camilli P. Direct interaction of the 170 kDa isoform of synaptojanin 1 with clathrin and with the clathrin adaptor AP-2. Current Biology 2000, 10: 471-474. PMID: 10801423, DOI: 10.1016/s0960-9822(00)00446-2.Peer-Reviewed Original ResearchConceptsClathrin adaptor AP-2Adaptor AP-2AP-2Synaptojanin 1Unique carboxy-terminal regionClathrin coat dynamicsAlpha-adaptin subunitCarboxy-terminal domainCarboxy-terminal extensionAmino-terminal domainSynaptic vesicle recyclingCarboxy-terminal regionBinding of clathrinReceptor-mediated endocytosisChinese hamster ovary cellsActin functionPolyphosphoinositide phosphataseEar domainClathrin coatHamster ovary cellsVesicle recyclingVariety of tissuesTransferrin uptakePleiotropic rolesClathrin
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 surfaceProteinAP-2 Recruitment to Synaptotagmin Stimulated by Tyrosine-Based Endocytic Motifs
Haucke V, De Camilli P. AP-2 Recruitment to Synaptotagmin Stimulated by Tyrosine-Based Endocytic Motifs. Science 1999, 285: 1268-1271. PMID: 10455054, DOI: 10.1126/science.285.5431.1268.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAnimalsBinding SitesCalcium-Binding ProteinsCattleCell MembraneCHO CellsClathrinCoated Pits, Cell-MembraneCricetinaeEndocytosisMembrane GlycoproteinsMembrane ProteinsNerve Tissue ProteinsNeuronsOligopeptidesPhospholipase DProtein BindingRatsRecombinant Fusion ProteinsSynaptic MembranesSynaptotagminsTyrosineConceptsAP-2 recruitmentEndocytic motifAP-2Cargo proteinsPlasma membraneTyrosine-based endocytic motifClathrin adaptor protein AP-2Adaptor protein AP-2Nucleation of clathrinNon-neuronal cellsProtein synaptotagminDocking siteSynaptotagminClathrinMotifProteinRecruitmentMembraneEndocytosisTyrosineBindingCellsPeptidesRecruitment 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 roleOmp25Protein
1998
Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis
Chen H, Fre S, Slepnev V, Capua M, Takei K, Butler M, Di Fiore P, De Camilli P. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis. Nature 1998, 394: 793-797. PMID: 9723620, DOI: 10.1038/29555.Peer-Reviewed Original ResearchAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsBlotting, NorthernBrainCalcium-Binding ProteinsCarrier ProteinsCHO CellsClathrinCricetinaeEndocytosisMembrane ProteinsMolecular Sequence DataNeuropeptidesPhosphoproteinsProtein BindingRatsRecombinant Fusion ProteinsTransfectionVesicular Transport Proteins
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