2022
SHIP164 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
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
1997
Identification and characterization of homologues of the Exocyst component Sec10p
Guo W, Roth D, Gatti E, De Camilli P, Novick P. Identification and characterization of homologues of the Exocyst component Sec10p. FEBS Letters 1997, 404: 135-139. PMID: 9119050, DOI: 10.1016/s0014-5793(97)00109-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCloning, MolecularCOS CellsExocytosisFungal ProteinsGolgi ApparatusHumansMammalsMolecular Sequence DataPolymerase Chain ReactionRecombinant ProteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTranscription, GeneticTransfectionVesicular Transport ProteinsConceptsC. elegans proteinsCharacterization of homologuesAmino acid identityBroad tissue distributionGolgi trafficMammalian counterpartsYeast SaccharomycesAcid identityGene productsCOS cellsWestern blot analysisSec10pPeripheral cytoplasmExocystBlot analysisProteinTissue distributionImmunofluorescence stainingSec8pCellsSaccharomycesCloningHomologuesExocytosisCytoplasm
1996
Phosphoinositides 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
Targeting of the 67-kDa Isoform of Glutamic Acid Decarboxylase to Intracellular Organelles Is Mediated by Its Interaction with the NH2-terminal Region of the 65-kDa Isoform of Glutamic Acid Decarboxylase (∗)
Dirkx R, Thomas A, Li L, Lernmark Å, Sherwin R, De Camilli P, Solimena M. Targeting of the 67-kDa Isoform of Glutamic Acid Decarboxylase to Intracellular Organelles Is Mediated by Its Interaction with the NH2-terminal Region of the 65-kDa Isoform of Glutamic Acid Decarboxylase (∗). Journal Of Biological Chemistry 1995, 270: 2241-2246. PMID: 7836456, DOI: 10.1074/jbc.270.5.2241.Peer-Reviewed Original ResearchConceptsGolgi complex regionNH2-terminal regionGlutamic acid decarboxylaseAbsence of palmitoylationSoluble cytosolic proteinsAcid decarboxylaseRegions of GAD65Cytosolic proteinsNeurotransmitter gamma-aminobutyric acidDetergent phasePerinuclear regionExtracts of brainIntracellular distributionGamma-aminobutyric acidPellet fractionComplex regionIsoformsProteinFibroblastsGAD67GAD65DecarboxylaseTriton XPalmitoylationNeurons