2022
Endoplasmic Reticulum Membrane Contact Sites, Lipid Transport, and Neurodegeneration.
Guillén-Samander A, De Camilli P. Endoplasmic Reticulum Membrane Contact Sites, Lipid Transport, and Neurodegeneration. Cold Spring Harbor Perspectives In Biology 2022, 15: a041257. PMID: 36123033, PMCID: PMC10071438, DOI: 10.1101/cshperspect.a041257.Peer-Reviewed Original ResearchConceptsMembrane contact sitesEndoplasmic reticulumEndoplasmic reticulum membrane contact sitesContact sitesLipid transportER membrane contact sitesCross talkLipid transfer proteinMutations of genesFamilial neurodegenerative diseasesIntracellular membranous organellesEndomembrane systemLipid trafficVesicular transportCell physiologyPlasma membraneMembranous organellesMembrane lipidsLipid exchangeTransfer proteinCell compartmentProteinNeurodegenerative diseasesMultiplicity of rolesDendritic tipsIn situ architecture of the lipid transport protein VPS13C at ER–lysosome membrane contacts
Cai S, Wu Y, Guillén-Samander A, Hancock-Cerutti W, Liu J, De Camilli P. In situ architecture of the lipid transport protein VPS13C at ER–lysosome membrane contacts. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2203769119. PMID: 35858323, PMCID: PMC9303930, DOI: 10.1073/pnas.2203769119.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumCryo-focused ion beam millingMembrane contact sitesCryo-electron tomographyFull-length structureLipid transport proteinsRod-like densitiesLysosome contactBinding partnerGenetic approachesHydrophobic grooveTransport proteinsContact sitesVps13Lipid transportAlphaFold predictionsFull-length modelHeLa cellsMembrane contactSitu architectureAdjacent membranesVPS13CProteinStructural informationEndo/lysosomesJIP3 links lysosome transport to regulation of multiple components of the axonal cytoskeleton
Rafiq N, Lyons L, Gowrishankar S, De Camilli P, Ferguson S. JIP3 links lysosome transport to regulation of multiple components of the axonal cytoskeleton. Communications Biology 2022, 5: 5. PMID: 35013510, PMCID: PMC8748971, DOI: 10.1038/s42003-021-02945-x.Peer-Reviewed Original Research
2021
VPS13D bridges the ER to mitochondria and peroxisomes via Miro
Guillén-Samander A, Leonzino M, Hanna MG, Tang N, Shen H, De Camilli P. VPS13D bridges the ER to mitochondria and peroxisomes via Miro. Journal Of Cell Biology 2021, 220: e202010004. PMID: 33891013, PMCID: PMC8077184, DOI: 10.1083/jcb.202010004.Peer-Reviewed Original ResearchConceptsLipid transport proteinsHigher eukaryotesER-mitochondriaSecretory pathwayAccessory factorsMitochondrial dynamicsDisease pathogenesisTransport proteinsParkin substratesLipid transferSplice variantsParkinson's disease pathogenesisVps13Lipid supplyMitochondriaMiroVPS13DERMESYeastMost lipidsTransport domainEukaryotesGem1MetazoansER
2020
Optimized Vivid-derived Magnets photodimerizers for subcellular optogenetics in mammalian cells
Benedetti L, Marvin JS, Falahati H, Guillén-Samander A, Looger LL, De Camilli P. Optimized Vivid-derived Magnets photodimerizers for subcellular optogenetics in mammalian cells. ELife 2020, 9: e63230. PMID: 33174843, PMCID: PMC7735757, DOI: 10.7554/elife.63230.Peer-Reviewed Original ResearchConceptsProtein fusion partnersSmall subcellular volumesSubcellular optogeneticsOrganelle contactsHomodimerization interfaceProtein modulesMammalian cellsBiological processesPhysiological processesSubcellular organellesLow temperature preincubationSimultaneous photoactivationFusion partnerCell preincubationWhole cellsSubcellular volumesConcatemerizationSpatial controlSpatiotemporal confinementCellsNeurosporaOrganellesHeterodimersVIVIDProtein
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 stateLipid transport by TMEM24 at ER–plasma membrane contacts regulates pulsatile insulin secretion
Lees JA, Messa M, Sun EW, Wheeler H, Torta F, Wenk MR, De Camilli P, Reinisch KM. Lipid transport by TMEM24 at ER–plasma membrane contacts regulates pulsatile insulin secretion. Science 2017, 355 PMID: 28209843, PMCID: PMC5414417, DOI: 10.1126/science.aah6171.Peer-Reviewed Original ResearchConceptsER–plasma membrane contactsLipid transportLipid-binding modulesMembrane contactPhosphoinositide signalingMembrane proteinsPrecursor phosphatidylinositolProtein 24Reversible localizationEndoplasmic reticulumTMEM24Β-cellsPhosphatidylinositolInsulin secretionCalcium oscillationsCytosolic calciumDephosphorylationType II diabetesPhosphorylationSignalingProteinReticulumSecretionII diabetesTransport
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
2015
PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER–plasma membrane contacts
Chung J, Torta F, Masai K, Lucast L, Czapla H, Tanner LB, Narayanaswamy P, Wenk MR, Nakatsu F, De Camilli P. PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER–plasma membrane contacts. Science 2015, 349: 428-432. PMID: 26206935, PMCID: PMC4638224, DOI: 10.1126/science.aab1370.Peer-Reviewed Original ResearchConceptsPlasma membraneEndoplasmic reticulumER integral membrane proteinsER–plasma membrane contactsMembrane lipid homeostasisIntegral membrane proteinsPleckstrin homology domainOxysterol-binding proteinPI4P phosphatase Sac1PI4P levelsCell membrane bilayerHomology domainPhosphatase Sac1Membrane proteinsORP8Function experimentsMembrane bilayerLipid homeostasisLipid transferProtein 5Membrane contactORP5PI4PPhosphatidylserineProtein
2004
Impaired PtdIns(4,5)P2 synthesis in nerve terminals produces defects in synaptic vesicle trafficking
Paolo G, Moskowitz HS, Gipson K, Wenk MR, Voronov S, Obayashi M, Flavell R, Fitzsimonds RM, Ryan TA, Camilli P. Impaired PtdIns(4,5)P2 synthesis in nerve terminals produces defects in synaptic vesicle trafficking. Nature 2004, 431: 415-422. PMID: 15386003, DOI: 10.1038/nature02896.Peer-Reviewed Original ResearchMeSH KeywordsAction PotentialsAnimalsBiological TransportCells, CulturedClathrinElectric ConductivityEndocytosisExocytosisGene DeletionKineticsMiceMice, KnockoutNeuronsPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)Presynaptic TerminalsSynaptic TransmissionSynaptic VesiclesConceptsClathrin coat dynamicsSynaptic vesicle cycleSynaptic vesicle exocytosisSynaptic vesicle traffickingSecond messenger moleculesEarly postnatal lethalityEndocytic intermediatesVesicle traffickingMembrane proteinsVesicle cycleVesicle exocytosisPostnatal lethalityCell regulationRecycling kineticsMessenger moleculesBiochemical studiesSynaptic defectsDirect interactionImportant functionsCritical roleMultiple stepsReleasable poolRegulationNerve terminalsDephosphorylation
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 role
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 analysisSeb1Phosphoinositides as Regulators in Membrane Traffic
De Camilli P, Emr S, McPherson P, Novick P. Phosphoinositides as Regulators in Membrane Traffic. Science 1996, 271: 1533-1539. PMID: 8599109, DOI: 10.1126/science.271.5255.1533.Peer-Reviewed Original ResearchConceptsMembrane trafficActivation of proteinsGuanosine triphosphatasesSignal transductionVesicular transportRegulatory mechanismsPhosphatidylinositol metabolitesSecond messengerLocation signalPhosphorylated productsCell surfaceClassical rolePhosphoinositideCritical rolePhosphatidylinositolTransductionTriphosphatasesRegulatorProteinMessengerRegulationPolar headRoleRecruitmentActivation
1995
Molecular mechanisms in synaptic vesicle recycling
De Camilli P. Molecular mechanisms in synaptic vesicle recycling. FEBS Letters 1995, 369: 3-12. PMID: 7641879, DOI: 10.1016/0014-5793(95)00739-v.Peer-Reviewed Original ResearchMeSH KeywordsBiological TransportCell CommunicationDynaminsEndocytosisExocytosisGTP PhosphohydrolasesMembranesModels, NeurologicalSynaptic VesiclesConceptsSynaptic vesicle recyclingVesicle recyclingSynaptic vesiclesMolecular mechanismsPowerful experimental modelVesicular trafficVesicle reformationNon-peptide neurotransmittersSecretory organellesRecycling pathwayHigh specializationVesiclesSpecialized formExocytosisRecent studiesNerve terminalsOrganellesMechanismRecyclingAbundanceCurrent informationPathwayUnique properties