2024
A complex of the lipid transport ER proteins TMEM24 and C2CD2 with band 4.1 at cell–cell contacts
Johnson B, Iuliano M, Lam T, Biederer T, De Camilli P. A complex of the lipid transport ER proteins TMEM24 and C2CD2 with band 4.1 at cell–cell contacts. Journal Of Cell Biology 2024, 223: e202311137. PMID: 39158698, PMCID: PMC11334333, DOI: 10.1083/jcb.202311137.Peer-Reviewed Original ResearchConceptsPlasma membraneNon-vesicular lipid transferSites of cell contactC-terminus motifsCell contact-dependent signalsContact-dependent signalingCell-cell contactER/PM junctionsTMEM24ER proteinsPM proteinsSynCAM 1Cell adhesion moleculesCellular functionsLipid transferC2CD2Phospholipid transportLipid transportCell contactProteinAdhesion moleculesCalcium homeostasisCellsFamily membersParalogs
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 tipsA 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 ResearchConceptsCaudate neuronsClinical manifestationsExposure of PtdSerPH domainMcLeod syndromeCell surface exposureER-PM contactsLipid dropletsTransport of lipidsPutative roleUnknown mechanismNeuronsLipid transfer proteinVPS13ALipid scramblasesTransfer proteinCytosolic loopExposurePlasma membraneCell surfaceEndoplasmic reticulumLipid transferERSyndromeDisease
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
Extended‐Synaptotagmins as Lipid Transporters at ER‐PM Contact Sites
Reinisch K, Schauder C, Wu X, Saheki Y, Narayanaswamy P, Torta F, Wenk M, De Camilli P. Extended‐Synaptotagmins as Lipid Transporters at ER‐PM Contact Sites. The FASEB Journal 2016, 30 DOI: 10.1096/fasebj.30.1_supplement.115.2.Peer-Reviewed Original ResearchMembrane contact sitesSMP domainContact sitesExtended synaptotagminsEndoplasmic reticulumPlasma membraneER-PM contact sitesLipid transportLipid transferLipid-binding modulesER-PM tethersΒ-barrel structureExchange of lipidsERMES complexE-SytsProtein modulesProtein domainsVesicular transportC2 domainÅ resolutionLipid transportersHydrophobic residuesUehara Memorial FoundationSynaptotagmin 2Direct role
2015
SMP-domain proteins at membrane contact sites: Structure and function
Reinisch KM, De Camilli P. SMP-domain proteins at membrane contact sites: Structure and function. Biochimica Et Biophysica Acta 2015, 1861: 924-927. PMID: 26686281, PMCID: PMC4902782, DOI: 10.1016/j.bbalip.2015.12.003.Peer-Reviewed Original ResearchConceptsMembrane contact sitesContact sitesAnant K. MenonCellular lipid landscapeTim P. LevineER-mitochondrial contactsSMP domainLipid landscapeComplex subunitsPlasma membraneMolecular basisLipid transportersEndoplasmic reticulumProteinRecent discoveryMembraneSuch sitesSitesSubunitsReticulumTransportersGlycerolipidsRegulationElucidationSpecial issueThe leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane
Baskin JM, Wu X, Christiano R, Oh MS, Schauder CM, Gazzerro E, Messa M, Baldassari S, Assereto S, Biancheri R, Zara F, Minetti C, Raimondi A, Simons M, Walther TC, Reinisch KM, De Camilli P. The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane. Nature Cell Biology 2015, 18: 132-138. PMID: 26571211, PMCID: PMC4689616, DOI: 10.1038/ncb3271.Peer-Reviewed Original ResearchPI4P/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 contactORP5PI4PPhosphatidylserineProteinPhosphoinositide Signaling in the Control of Membrane Dynamics and Interactions
De Camilli P. Phosphoinositide Signaling in the Control of Membrane Dynamics and Interactions. The FASEB Journal 2015, 29 DOI: 10.1096/fasebj.29.1_supplement.90.1.Peer-Reviewed Original ResearchPlasma membraneEndoplasmic reticulumIntrinsic membrane proteinsKey regulatory roleIntracellular second messengerMembrane identityE-SytsExtended synaptotagminsDifferent phosphoinositidesEndocytic membranesPutative functionsMembrane proteinsCell physiologyMembrane dynamicsCytosolic proteinsSecond messengerRegulatory rolePhosphatidyl inositolPhosphoinositideCell membraneInositol groupProteinMembranePhosphorylated metabolitesCa 2
2014
Manipulation of Plasma Membrane Phosphoinositides Using Photoinduced Protein–Protein Interactions
Idevall-Hagren O, De Camilli P. Manipulation of Plasma Membrane Phosphoinositides Using Photoinduced Protein–Protein Interactions. Methods In Molecular Biology 2014, 1148: 109-128. PMID: 24718798, DOI: 10.1007/978-1-4939-0470-9_8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsArabidopsis ProteinsCatalytic DomainCell MembraneChlorocebus aethiopsCOS CellsCryptochromesHeLa CellsHumansLightMiceMolecular Sequence DataPhosphatidylinositolsPhosphoric Monoester HydrolasesPhotochemical ProcessesProtein Interaction Domains and MotifsProtein MultimerizationRecombinant Fusion ProteinsConceptsPlasma membraneCryptochrome 2Plasma membrane phosphatidylinositolProtein-protein interactionsLight-dependent conversionLipid-binding domainLive-cell imagingCritical regulatory roleMembrane lipid metabolismPhosphoinositide speciesSpatiotemporal regulationDimerization moduleCell physiologyMembrane phosphatidylinositolRegulatory roleTypes of cellsInositol phospholipidsPhosphorylated productsDimerization methodLipid metabolismMembraneCIB1DephosphorylationPhosphatidylinositolPhosphoinositide
2008
Molecular mechanisms in endocytosis at neuronal synapses
De Camilli P. Molecular mechanisms in endocytosis at neuronal synapses. The FASEB Journal 2008, 22: 250.3-250.3. DOI: 10.1096/fasebj.22.1_supplement.250.3.Peer-Reviewed Original ResearchFunction of dynaminNeuronal synapsesPowerful model systemRole of isoformsGTPase dynaminEndocytic proteinsEndocytic recyclingPlasma membraneMolecular mechanismsSecretory systemReconstitution experimentsEndocytosisSynaptic vesiclesHigh specializationDynaminLipid membranesRelease of neurotransmittersModel systemProteinMembraneFundamental mechanismsComplementary approachesRecent advancesDephosphorylationOrganelles
2000
A Functional Link between Dynamin and the Actin Cytoskeleton at Podosomes
Ochoa G, Slepnev V, Neff L, Ringstad N, Takei K, Daniell L, Kim W, Cao H, McNiven M, Baron R, De Camilli P. A Functional Link between Dynamin and the Actin Cytoskeleton at Podosomes. Journal Of Cell Biology 2000, 150: 377-390. PMID: 10908579, PMCID: PMC2180219, DOI: 10.1083/jcb.150.2.377.Peer-Reviewed Original ResearchConceptsDynamin 2Rous sarcoma virus resultsFunctional linkAttachment sitesDynamin familyActin cytoskeletonActin turnoverGFP-actinAdhesion structuresPlasma membranePodosomesAdhesion plaquesDynaminCell transformationNontransformed cellsTubular invaginationsFluorescence recoverySimilar turnoverActinSubstratumVirus resultsCellsTurnoverCytoskeletonDramatic changes
1999
AP-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 siteSynaptotagminClathrinMotifProteinRecruitmentMembraneEndocytosisTyrosineBindingCellsPeptides
1998
Perturbation of Dynamin II with an Amphiphysin SH3 Domain Increases GLUT4 Glucose Transporters at the Plasma Membrane in 3T3-L1 Adipocytes DYNAMIN II PARTICIPATES IN GLUT4 ENDOCYTOSIS*
Volchuk A, Narine S, Foster L, Grabs D, De Camilli P, Klip A. Perturbation of Dynamin II with an Amphiphysin SH3 Domain Increases GLUT4 Glucose Transporters at the Plasma Membrane in 3T3-L1 Adipocytes DYNAMIN II PARTICIPATES IN GLUT4 ENDOCYTOSIS*. Journal Of Biological Chemistry 1998, 273: 8169-8176. PMID: 9525921, DOI: 10.1074/jbc.273.14.8169.Peer-Reviewed Original ResearchConceptsGLUT4 endocytosisDynamin IIGLUT4 glucose transportersPlasma membraneCell surfaceSH3 domainClathrin-coated vesicle formationFusion proteinGlucose transporterLevels of GLUT4Amphiphysin SH3 domainLow-density microsomal fractionIsolated plasma membranesTransferrin endocytosisEndocytic systemGLUT4 internalizationProtein dynaminGlutathione S-transferaseEndosomal compartmentsGLUT4 distributionVesicle formationDynamin peptideEndocytosisGLUT4S-transferase
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