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 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
2012
Dynamin 2 regulates S1P1 signalling and T cell migration (173.15)
Willinger T, Ferguson S, De Camilli P, Flavell R. Dynamin 2 regulates S1P1 signalling and T cell migration (173.15). The Journal Of Immunology 2012, 188: 173.15-173.15. DOI: 10.4049/jimmunol.188.supp.173.15.Peer-Reviewed Original ResearchDynamin 2Cell egressCell migrationT cell-specific deletionT cell egressReceptor-mediated endocytosisVesicle scissionLarge GTPaseCell-specific deletionCell motilityT cell migrationUnexpected roleReceptor internalizationCell surfaceSphingosine 1General defectDynaminAgonist stimulationMigratory responseEndocytosisS1P receptorsThymic egressCritical roleEgressS1P1
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 surfaceProtein
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
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