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 ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAnimalsClathrinEndocytosisHumansMembrane ProteinsSynaptic VesiclesConceptsAccessory 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 vesiclesSubunitsMu2Tandem 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 arrangementDirect 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 siteSynaptotagminClathrinMotifProteinRecruitmentMembraneEndocytosisTyrosineBindingCellsPeptidesThe 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
1998
Role of Phosphorylation in Regulation of the Assembly of Endocytic Coat Complexes
Slepnev V, Ochoa G, Butler M, Grabs D, De Camilli P. Role of Phosphorylation in Regulation of the Assembly of Endocytic Coat Complexes. Science 1998, 281: 821-824. PMID: 9694653, DOI: 10.1126/science.281.5378.821.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Protein Complex beta SubunitsAdaptor Proteins, Vesicular TransportAdenosine TriphosphateAnimalsBinding SitesCarbazolesChromatography, AffinityClathrinCyclosporineDimerizationDynamin IDynaminsEndocytosisEnzyme InhibitorsGTP PhosphohydrolasesIndole AlkaloidsMembrane ProteinsNerve Tissue ProteinsPhosphoric Monoester HydrolasesRatsRecombinant Fusion ProteinsSrc Homology DomainsEpsin 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