2022
A partnership between the lipid scramblase XK and the lipid transfer protein VPS13A at the plasma membrane
Guillén-Samander A, Wu Y, Pineda SS, García FJ, Eisen JN, Leonzino M, Ugur B, Kellis M, Heiman M, De Camilli P. A partnership between the lipid scramblase XK and the lipid transfer protein VPS13A at the plasma membrane. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2205425119. PMID: 35994651, PMCID: PMC9436381, DOI: 10.1073/pnas.2205425119.Peer-Reviewed Original ResearchMeSH KeywordsCarrier ProteinsCell MembraneEndoplasmic ReticulumHumansLipidsNeuroacanthocytosisVesicular Transport ProteinsConceptsCaudate neuronsClinical manifestationsExposure of PtdSerPH domainMcLeod syndromeCell surface exposureER-PM contactsLipid dropletsTransport of lipidsPutative roleUnknown mechanismNeuronsLipid transfer proteinVPS13ALipid scramblasesTransfer proteinCytosolic loopExposurePlasma membraneCell surfaceEndoplasmic reticulumLipid transferERSyndromeDiseaseSHIP164 is a chorein motif lipid transfer protein that controls endosome–Golgi membrane traffic
Hanna MG, Suen PH, Wu Y, Reinisch KM, De Camilli P. SHIP164 is a chorein motif lipid transfer protein that controls endosome–Golgi membrane traffic. Journal Of Cell Biology 2022, 221: e202111018. PMID: 35499567, PMCID: PMC9067936, DOI: 10.1083/jcb.202111018.Peer-Reviewed Original ResearchMeSH KeywordsCarrier ProteinsEndosomesGolgi ApparatusIntracellular MembranesIntracellular Signaling Peptides and ProteinsLipidsConceptsMannose-6-phosphate receptorCation-independent mannose-6-phosphate receptorMembrane contact sitesEarly endocytic pathwayGolgi membrane trafficLipid transfer proteinLipid transfer propertiesProtein-lipid ratioMembrane cargoMembrane trafficEndocytic membranesVesicular trafficRetrograde trafficEndocytic pathwayFunctional characterizationContact sitesMembranous organellesGolgi complexVesicle clustersCellular membranesTransfer proteinProteinLipid compositionOrganellesMembrane
2017
Endoplasmic Reticulum—Plasma Membrane Contact Sites
Saheki Y, De Camilli P. Endoplasmic Reticulum—Plasma Membrane Contact Sites. Annual Review Of Biochemistry 2017, 86: 1-26. PMID: 28301744, DOI: 10.1146/annurev-biochem-061516-044932.Peer-Reviewed Original ResearchConceptsPlasma membraneEndoplasmic reticulumProtein tethersEndoplasmic reticulum-plasma membrane contact sitesNonvesicular lipid transportER-PM contactsMembrane contact sitesLipid transfer proteinLipid trafficCell physiologyContact sitesMembranous organellesLipid transportBroad localizationTransfer proteinCross talkIntracellular CaDirect physical contactMultiplicity of rolesFunctional state
2016
Control of plasma membrane lipid homeostasis by the extended synaptotagmins
Saheki Y, Bian X, Schauder CM, Sawaki Y, Surma MA, Klose C, Pincet F, Reinisch KM, De Camilli P. Control of plasma membrane lipid homeostasis by the extended synaptotagmins. Nature Cell Biology 2016, 18: 504-515. PMID: 27065097, PMCID: PMC4848133, DOI: 10.1038/ncb3339.Peer-Reviewed Original ResearchConceptsSMP domainE-Syt1ER-PM tethersMembrane lipid homeostasisPlasma membrane lipidsEndoplasmic reticulum proteinAccumulation of diacylglycerolE-SytsExtended synaptotagminsMolecular basisMajor glycerolipidsReticulum proteinsMetabolic recyclingMembrane lipidsLipid homeostasisPLC activationSynaptotagminSustained accumulationHomeostatic responseDiacylglycerolGlycerolipidsMetabolic changesGenomeCa2Accumulation
2001
Generation of high curvature membranes mediated by direct endophilin bilayer interactions
Farsad K, Ringstad N, Takei K, Floyd S, Rose K, De Camilli P. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. Journal Of Cell Biology 2001, 155: 193-200. PMID: 11604418, PMCID: PMC2198845, DOI: 10.1083/jcb.200107075.Peer-Reviewed Original ResearchMeSH KeywordsAcyltransferasesAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsBiological TransportCarrier ProteinsCell MembraneCell SizeDynaminsGolgi ApparatusGTP PhosphohydrolasesHumansLipid BilayersMacromolecular SubstancesMolecular Sequence DataNerve Tissue ProteinsPhylogenyProtein Structure, TertiaryRatsSequence Homology, Amino AcidSynaptic VesiclesConceptsEndophilin-1Lipid bilayersMembrane-trafficking eventsAmino acid stretchHigh-curvature membranesNH2-terminal regionCell-free systemEndophilin BEndophilin functionGTPase dynaminDynamin ringsVesicle buddingEndophilinEndocytic vesiclesGolgi complexNarrow tubulesMembrane deformationCorresponding regionProteinTransferase activityAcyl transferase activityBilayer interactionsNew insightsLipid tubulesPotential roleDifferential Expression of Endophilin 1 and 2 Dimers at Central Nervous System Synapses*
Ringstad N, Nemoto Y, De Camilli P. Differential Expression of Endophilin 1 and 2 Dimers at Central Nervous System Synapses*. Journal Of Biological Chemistry 2001, 276: 40424-40430. PMID: 11518713, DOI: 10.1074/jbc.m106338200.Peer-Reviewed Original ResearchConceptsEndophilin-1SH3 domain-mediated interactionsDiverse cellular proteinsDomain-mediated interactionsSynaptic vesicle biogenesisNH2-terminal moietyCoiled-coil domainCentral nervous system synapsesGTPase dynaminVesicle biogenesisDifferent cellular targetsEndocytic machineryCellular proteinsSynaptojanin 1Endophilin isoformsRelated proteinsDifferential expressionCellular targetsStable dimerSynaptojaninDynaminSame complexProteinCentral synapsesFamily members
2000
Synaptic Autoimmunity and the Salk Factor
Solimena M, De Camilli P. Synaptic Autoimmunity and the Salk Factor. Neuron 2000, 28: 309-316. PMID: 11144336, DOI: 10.1016/s0896-6273(00)00105-7.Peer-Reviewed Original ResearchFission and Uncoating of Synaptic Clathrin-Coated Vesicles Are Perturbed by Disruption of Interactions with the SH3 Domain of Endophilin
Gad H, Ringstad N, Löw P, Kjaerulff O, Gustafsson J, Wenk M, Di Paolo G, Nemoto Y, Crum J, Ellisman M, De Camilli P, Shupliakov O, Brodin L. Fission and Uncoating of Synaptic Clathrin-Coated Vesicles Are Perturbed by Disruption of Interactions with the SH3 Domain of Endophilin. Neuron 2000, 27: 301-312. PMID: 10985350, DOI: 10.1016/s0896-6273(00)00038-6.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsBinding, CompetitiveCarrier ProteinsClathrinCloning, MolecularCoated Pits, Cell-MembraneDynaminsGTP PhosphohydrolasesLampreysMicroinjectionsMolecular Sequence DataNerve Tissue ProteinsPeptide FragmentsPhosphoric Monoester HydrolasesSequence Homology, Amino AcidSrc Homology DomainsSynaptic VesiclesConceptsProline-rich domainSynaptic vesicle endocytosisSH3 domainVesicle endocytosisEndophilin's SH3 domainClathrin coat formationClathrin-coated vesiclesClathrin-coated pitsDisruption of interactionsEndocytic intermediatesProteinprotein interactionsCoat formationEndophilinMolecular switchUncoatingEndocytosisVesiclesAutoimmunity 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 membraneGephyrinSpasmSyndromeSynapsesAutoantibodiesPatientsGABAEpsin 1 Undergoes Nucleocytosolic Shuttling and Its Eps15 Interactor Nh2-Terminal Homology (Enth) Domain, Structurally Similar to Armadillo and Heat Repeats, Interacts with the Transcription Factor Promyelocytic Leukemia Zn2+ Finger Protein (Plzf)
Hyman J, Chen H, Di Fiore P, De Camilli P, Brunger A. Epsin 1 Undergoes Nucleocytosolic Shuttling and Its Eps15 Interactor Nh2-Terminal Homology (Enth) Domain, Structurally Similar to Armadillo and Heat Repeats, Interacts with the Transcription Factor Promyelocytic Leukemia Zn2+ Finger Protein (Plzf). Journal Of Cell Biology 2000, 149: 537-546. PMID: 10791968, PMCID: PMC2174850, DOI: 10.1083/jcb.149.3.537.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsArmadillo Domain ProteinsBeta CateninCalcium-Binding ProteinsCarrier ProteinsCell LineCell NucleusCrystallography, X-RayCytoskeletal ProteinsCytosolDNA-Binding ProteinsDrosophila ProteinsFluorescent Antibody TechniqueInsect ProteinsModels, MolecularMolecular Sequence DataNeuropeptidesPhosphoproteinsProtein BindingRatsSequence AlignmentTrans-ActivatorsTranscription FactorsVesicular Transport ProteinsZinc FingersConceptsENTH domainFinger proteinCRM1-dependent nuclear export pathwayClathrin adaptor AP-2Nuclear export pathwayAdaptor AP-2HEAT repeatsEndocytic machineryNuclear functionsHomology domainExport pathwayLeptomycin BEpsin 1AP-2Cytosolic proteinsUnknown functionDirect interactionEpsinTerminal portionClathrinProteinArmadillosAntifungal antibioticsPathwayDomain
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 stagesCoatMachineryInvaginationEpidermal growth factor pathway substrate 15, Eps15
Salcini A, Chen H, Iannolo G, De Camilli P, Di Fiore P. Epidermal growth factor pathway substrate 15, Eps15. The International Journal Of Biochemistry & Cell Biology 1999, 31: 805-809. PMID: 10481267, DOI: 10.1016/s1357-2725(99)00042-4.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsCalcium-Binding ProteinsCarrier ProteinsCell LineChromosomes, Human, Pair 1EndocytosisEpidermal Growth FactorHumansIntracellular Signaling Peptides and ProteinsNeuropeptidesPhosphoproteinsSignal TransductionTransferrinVesicular Transport ProteinsConceptsEpidermal growth factor receptorPutative coiled-coil regionCoiled-coil regionCell proliferationNIH 3T3 cellsReceptor-mediated endocytosisEH domainNH2-terminal portionEndocytic machineryEpsin functionIntracellular sortingEps15Growth factor receptorTerminal domainAP-2Kinase activityBinding proteinMultiple copiesBiomolecular strategiesProteinFactor receptorTripartite structureMLL geneGenesProliferationRecruitment 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
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
1997
The SH3p4/Sh3p8/SH3p13 protein family: Binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain
Ringstad N, Nemoto Y, De Camilli P. The SH3p4/Sh3p8/SH3p13 protein family: Binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 8569-8574. PMID: 9238017, PMCID: PMC23017, DOI: 10.1073/pnas.94.16.8569.Peer-Reviewed Original ResearchConceptsSrc homology 3 domainSynaptic vesicle recyclingDynamin IProtein familyVesicle recyclingSH3 domain-containing proteinsDomain-containing proteinsProline-rich domainTwo-hybrid methodPhysiological binding partnerProline-rich tailRat brain libraryFurther biochemical studiesSH3 domainSynaptojaninDynamin I.Nerve terminal proteinBinding partnerTerminal proteinAmphiphysin IRelated proteinsBrain libraryMultiple tissuesBiochemical studiesProteinAmphiphysin 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
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
1988
[17] Type II cAMP-dependent protein kinase regulatory subunit-binding proteins
Lohmann S, De Camilli P, Walter U. [17] Type II cAMP-dependent protein kinase regulatory subunit-binding proteins. Methods In Enzymology 1988, 159: 183-193. PMID: 2842584, DOI: 10.1016/0076-6879(88)59019-5.Peer-Reviewed Original ResearchConceptsRII subunitsCytosolic cAMP-dependent protein kinaseAdditional proteinsType II cAMP-dependent proteinCAMP-dependent protein kinaseCAMP-dependent proteinMicrotubule-associated proteinsRII overlayProtein kinaseSDS-polyacrylamide gel electrophoresisCertain proteinsNative stateProteinSteps of purificationGel electrophoresisSubunitsCellular structureAssay conditionsNonspecific interactionsRIIHigh affinityHigh enough affinityLight microscopyKinaseAffinity