2001
PIP Kinase Iγ Is the Major PI(4,5)P2 Synthesizing Enzyme at the Synapse
Wenk M, Pellegrini L, Klenchin V, Di Paolo G, Chang S, Daniell L, Arioka M, Martin T, De Camilli P. PIP Kinase Iγ Is the Major PI(4,5)P2 Synthesizing Enzyme at the Synapse. Neuron 2001, 32: 79-88. PMID: 11604140, DOI: 10.1016/s0896-6273(01)00456-1.Peer-Reviewed Original ResearchConceptsSynaptojanin 1Clathrin-coated intermediatesPolyphosphoinositide phosphatase synaptojanin-1Coat recruitmentActin functionClathrin coatPositive regulatorEndocytic zonesPIPKIgammaSynthesizing enzymesRecruitmentIgammaSynapseDephosphorylationEndocytosisMajor brainElevated levelsRegulatorProteinActinEnzymeMembrane
2000
Accessory factors in clathrin-dependent synaptic vesicle endocytosis
Slepnev V, De Camilli P. Accessory factors in clathrin-dependent synaptic vesicle endocytosis. Nature Reviews Neuroscience 2000, 1: 161-172. PMID: 11257904, DOI: 10.1038/35044540.Peer-Reviewed Original ResearchConceptsAccessory factorsNumerous accessory proteinsSynaptic vesicle endocytosisClathrin-mediated endocytosisRecent structural studiesPlasma membrane componentsSynaptic vesicle recyclingInternalization of receptorsVesicle endocytosisCoat assemblyExtracellular ligandsClathrin coatMolecular detailsVesicle recyclingAccessory proteinsGenetic studiesEndocytosisMembrane componentsSurface proteinsClathrinStructural studiesProteinVesiclesInternalizationNew aspectsDual 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 vesiclesSubunitsMu2Direct 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 surfaceProteinEndophilin/SH3p4 Is Required for the Transition from Early to Late Stages in Clathrin-Mediated Synaptic Vesicle Endocytosis
Ringstad N, Gad H, Löw P, Di Paolo G, Brodin L, Shupliakov O, De Camilli P. Endophilin/SH3p4 Is Required for the Transition from Early to Late Stages in Clathrin-Mediated Synaptic Vesicle Endocytosis. Neuron 1999, 24: 143-154. PMID: 10677033, DOI: 10.1016/s0896-6273(00)80828-4.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsAntibodiesCaenorhabditis elegansCarrier ProteinsCell-Free SystemClathrinCoated Pits, Cell-MembraneDynaminsEndocytosisGTP PhosphohydrolasesLampreysMicroscopy, ElectronMolecular Sequence DataRatsSpinal CordSrc Homology DomainsSynapsesSynaptic VesiclesConceptsSynaptic vesicle endocytosisVesicle endocytosisClathrin coatClathrin-coated pitsSynaptic vesicle recyclingCell-free systemEndophilin functionGTPase dynaminFunctional partnersVesicle fissionBiochemical machineryVesicle recyclingSH3p4EndophilinDynaminEndocytosisAntibody-mediated disruptionProteinActive zoneSynaptojaninClathrinLater stagesCoatMachineryInvaginationFunctional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
Takei K, Slepnev V, Haucke V, De Camilli P. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nature Cell Biology 1999, 1: 33-39. PMID: 10559861, DOI: 10.1038/9004.Peer-Reviewed Original ResearchConceptsDynamin 1Functional partnershipCell-free systemAmphiphysin 1Clathrin coatDynaminAmphiphysinRing-like structurePresence of GTPSynaptic vesiclesEndocytosisNarrow tubulesLipid bilayersMorphological evidenceBilayer curvatureVesiclesSpherical liposomesPotential functionClathrinGTPDirect morphological evidenceProteinAssembles
1997
Recycling of Synaptic Vesicles
Bauerfeind R, David C, Grabs D, McPherson P, Nemoto Y, Slepnev V, Takei K, De Camilli P. Recycling of Synaptic Vesicles. Advances In Pharmacology 1997, 42: 253-257. PMID: 9327892, DOI: 10.1016/s1054-3589(08)60741-3.Peer-Reviewed Original ResearchConceptsSynaptic vesicle endocytosisSynaptic vesicle recyclingVesicle endocytosisVesicle recyclingSynaptic vesiclesPlasma membraneClathrin adaptor complex AP2Vesicular transport stepsClathrin-coated vesiclesClathrin-coated pitsMicrotubule-binding proteinSynaptic vesicle cycleRole of proteinsCell surface receptorsRole of lipidsClathrin coatRestrictive temperatureEarly endosomesGuanosine triphosphataseRecycling pathwayVesicle cycleDynaminTransport stepsEndocytosisSurface receptors