2023
Force redistribution in clathrin-mediated endocytosis revealed by coiled-coil force sensors
Ren Y, Yang J, Fujita B, Jin H, Zhang Y, Berro J. Force redistribution in clathrin-mediated endocytosis revealed by coiled-coil force sensors. Science Advances 2023, 9: eadi1535. PMID: 37831774, PMCID: PMC10575576, DOI: 10.1126/sciadv.adi1535.Peer-Reviewed Original ResearchConceptsActin cytoskeletonPlasma membraneHuntingtin Interacting Protein 1Clathrin-mediated endocytosisCountless cellular processesEndocytic machineryCellular processesClathrin latticesProtein condensationCytoskeletonEnd4pProtein 1Membrane deformationPiconewton forcesEndocytosisVivo force measurementsMembranePiconewtonsClathrinMachineryProteinCoatMolecular scaleInsights of Endocytosis Signaling in Health and Disease
Pathak C, Vaidya F, Waghela B, Jaiswara P, Gupta V, Kumar A, Rajendran B, Ranjan K. Insights of Endocytosis Signaling in Health and Disease. International Journal Of Molecular Sciences 2023, 24: 2971. PMID: 36769293, PMCID: PMC9918140, DOI: 10.3390/ijms24032971.Peer-Reviewed Original ResearchConceptsEndocytic machineryPlasma membraneCellular defenseFundamental cellular machinerySignal transduction modulesDifferent cellular compartmentsVital physiological processesProcess of endocytosisEndocytic proteinsIndependent endocytosisEndocytosis machineryTransduction modulesEukaryotic cellsCaveolar pathwayCellular machineryMammalian cellsEndocytic pathwayCell divisionCellular compartmentsComplex proteinsFunctional characterizationPhysiological processesMachinery resultsHuman diseasesEndocytosis
2022
Podocyte Endocytosis in Regulating the Glomerular Filtration Barrier
Tian X, Bunda P, Ishibe S. Podocyte Endocytosis in Regulating the Glomerular Filtration Barrier. Frontiers In Medicine 2022, 9: 801837. PMID: 35223901, PMCID: PMC8866310, DOI: 10.3389/fmed.2022.801837.Peer-Reviewed Original ResearchPlasma membrane componentsHuman genetic mutationsGlomerular filtration barrierEndocytosis genesEndocytic machineryFiltration barrierTransmembrane receptorsBiological functionsVesicle formationSignaling pathwaysEndocytosisMembrane componentsPodocyte functionCellular endocytosisNovel insightsProteinuric glomerular diseasesAdjacent basement membraneGenetic mutationsFunction studiesEpithelial cellsPathwayEndothelial cell layerBasement membraneImportant roleCell layer
2019
Lysosome-Rich Enterocytes Mediate Protein Absorption in the Vertebrate Gut
Park J, Levic DS, Sumigray KD, Bagwell J, Eroglu O, Block CL, Eroglu C, Barry R, Lickwar CR, Rawls JF, Watts SA, Lechler T, Bagnat M. Lysosome-Rich Enterocytes Mediate Protein Absorption in the Vertebrate Gut. Developmental Cell 2019, 51: 7-20.e6. PMID: 31474562, PMCID: PMC6783362, DOI: 10.1016/j.devcel.2019.08.001.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsApoptosis Regulatory ProteinsDietary ProteinsDisease Models, AnimalEnterocytesFemaleGastrointestinal MicrobiomeGene DeletionGene Expression Regulation, DevelopmentalIleumIntestinal AbsorptionIntestinesKwashiorkorLigandsLysosomesMaleMembrane ProteinsMiceReceptors, Cell SurfaceZebrafishZebrafish ProteinsConceptsFluid-phase endocytosisEndocytic machineryTrans-cellular transportLuminal protein digestionVertebrate gutLarval zebrafishCritical developmental stagesStomachless fishMolecular mechanismsVertebrate growthProtein uptakeDevelopmental stagesIntracellular digestionProtein digestionConditional deletionStunted growthIntestinal cellsOral acquisitionDab2Dietary proteinSevere protein malnutritionDigestive functionNeonatal mammalsProteinMalnutrition syndrome
2017
Clathrin Assembly Defines the Onset and Geometry of Cortical Patterning
Yang Y, Xiong D, Pipathsouk A, Weiner OD, Wu M. Clathrin Assembly Defines the Onset and Geometry of Cortical Patterning. Developmental Cell 2017, 43: 507-521.e4. PMID: 29161594, PMCID: PMC5826602, DOI: 10.1016/j.devcel.2017.10.028.Peer-Reviewed Original ResearchConceptsPlasma membraneClathrin assemblyClathrin functionEndocytic proteinsMembrane traffickingEndocytic machineryN-WASPEndocytic eventsSignal transductionDownstream factorsCell surfaceCortical patterningPattern formationAssemblyMembraneImportant insightsActive processSingle-cell patternFBP17Cdc42ClathrinEndocytosisTransductionCortical pattern formationPhosphatidylinositol
2008
Interaction of Campylobacter jejuni with Host Cells
Watson R, Galán J. Interaction of Campylobacter jejuni with Host Cells. 2008, 287-296. DOI: 10.1128/9781555815554.ch16.Peer-Reviewed Original ResearchHost cellsBacterial internalizationCell biologyHost cell gene expressionVesicular trafficking pathwaysPowerful genetic toolsCell gene expressionEndocytic machineryTrafficking pathwaysStrong phenotypeGenetic toolsCampylobacter jejuniJejuni mutantsGene expressionIntestinal epithelial cellsMicrobial pathogensInnate immune responseNonphagocytic cellsOwn uptakeBacterial determinantsSpecific adaptationsIntracellular pathogensMutantsPathogenic bacteriaCell interactions
2005
Caenorhabditus elegans Arrestin Regulates Neural G Protein Signaling and Olfactory Adaptation and Recovery*
Palmitessa A, Hess HA, Bany IA, Kim YM, Koelle MR, Benovic JL. Caenorhabditus elegans Arrestin Regulates Neural G Protein Signaling and Olfactory Adaptation and Recovery*. Journal Of Biological Chemistry 2005, 280: 24649-24662. PMID: 15878875, DOI: 10.1074/jbc.m502637200.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAmino Acid SequenceAnimalsAnimals, Genetically ModifiedArrestinBenzaldehydesBlotting, NorthernCaenorhabditis elegansCell LineCells, CulturedChemotaxisClathrinCOS CellsDiacetylEndocytosisExonsGreen Fluorescent ProteinsGTP-Binding ProteinsHumansImmunohistochemistryModels, GeneticMolecular Sequence DataMutationNeuronsOdorantsOlfactory PathwaysPentanolsPhenotypePhylogenyProtein BindingProtein Structure, TertiarySequence Analysis, DNASignal TransductionTime FactorsConceptsARR-1Receptor endocytosisG protein signalingG protein-coupled receptorsOlfactory adaptationVolatile odorantsProtein-coupled receptorsPotential mechanistic basisEndocytic machineryCaenorhabditis elegansNull mutantsHSN neuronsProtein signalingReceptor kinaseAdaptation defectRecovery defectArrestin functionChemosensory neuronsEnvironmental cuesBind proteinsMechanistic basisVivo linkTransgenic expressionArrestinNormal chemotaxis
2003
The tetraspanin CD63 enhances the internalization of the H,K-ATPase β-subunit
Duffield A, Kamsteeg EJ, Brown AN, Pagel P, Caplan MJ. The tetraspanin CD63 enhances the internalization of the H,K-ATPase β-subunit. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 15560-15565. PMID: 14660791, PMCID: PMC307607, DOI: 10.1073/pnas.2536699100.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDChlorocebus aethiopsCloning, MolecularCOS CellsGene LibraryH(+)-K(+)-Exchanging ATPaseHumansKidneyMembrane ProteinsModels, BiologicalPlatelet Membrane GlycoproteinsProtein SubunitsProtein TransportRabbitsRatsRats, Sprague-DawleyRecombinant ProteinsTetraspanin 30TransfectionConceptsAdaptor protein complex 2Intracellular compartmentsK-ATPaseTetraspanin CD63K-ATPase β-subunitCOS-7 cellsEndocytic machineryAdaptor proteinLate endosomesSecretory vesiclesPlasma membraneGastric parietal cellsBiochemical experimentsInteraction partnersΒ-subunitParietal cellsCell surfaceEnhanced endocytosisTubulovesicular elementsCD63CompartmentsCellsInternalizationComplexes 2Endosomes
2001
Differential 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 membersThe Eps15 C. elegans homologue EHS-1 is implicated in synaptic vesicle recycling
Salcini A, Hilliard M, Croce A, Arbucci S, Luzzi P, Tacchetti C, Daniell L, De Camilli P, Pelicci P, Di Fiore P, Bazzicalupo P. The Eps15 C. elegans homologue EHS-1 is implicated in synaptic vesicle recycling. Nature Cell Biology 2001, 3: 755-760. PMID: 11483962, DOI: 10.1038/35087075.Peer-Reviewed Original ResearchMeSH KeywordsAldicarbAnimalsAnimals, Genetically ModifiedCaenorhabditis elegansCalcium-Binding ProteinsDynaminsFluorescent Antibody TechniqueGanglia, InvertebrateGene DeletionGenes, ReporterGTP PhosphohydrolasesInsecticidesMicroscopy, ElectronMolecular Sequence DataMovement DisordersMutationNerve Tissue ProteinsNervous SystemPhenotypePhosphoproteinsProtein TransportSequence Homology, Nucleic AcidSynaptic VesiclesTemperatureConceptsSynaptic vesicle recyclingVesicle recyclingEHS-1Protein-protein interactionsMammalian Eps15Dynamin proteinsEH domainEndocytic machineryEps15Mutant formsPermissive temperatureFunctional studiesSynaptic vesiclesDynaminUncoordinated movementsPresynaptic defectsProteinPhenotypeOrthologuesCaenorhabditisWormsGenesNematodesMachineryVesicles
2000
Simian Immunodeficiency Virus Containing Mutations in N-Terminal Tyrosine Residues and in the PxxP Motif in Nef Replicates Efficiently in Rhesus Macaques
Carl S, Iafrate A, Lang S, Stolte N, Stahl-Hennig C, Mätz-Rensing K, Fuchs D, Skowronski J, Kirchhoff F. Simian Immunodeficiency Virus Containing Mutations in N-Terminal Tyrosine Residues and in the PxxP Motif in Nef Replicates Efficiently in Rhesus Macaques. Journal Of Virology 2000, 74: 4155-4164. PMID: 10756028, PMCID: PMC111930, DOI: 10.1128/jvi.74.9.4155-4164.2000.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesCD4 AntigensCell Line, TransformedCOS CellsDown-RegulationGene Products, nefHistocompatibility Antigens Class IHumansMacaca mulattaMutagenesisp21-Activated KinasesPhosphorylationProtein Serine-Threonine KinasesSimian immunodeficiency virussrc Homology DomainsTyrosineViral LoadVirus ReplicationConceptsAbility of NefTyrosine-based endocytosis signalTyrosine residuesHigh viral loadCellular signal transductionTyrosine kinase SrcNef functionViral loadEndocytosis signalEndocytic machineryPXXP motifN-terminal tyrosine residueCell surface expressionKinase SrcKinase assaysSignal transductionProline residuesClass I major histocompatibility complexN-terminal tyrosineI major histocompatibility complexLigand domainCombined mutationsNef interactionsMajor histocompatibility complexMutationsEpsin 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 Calcineurin-Dynamin 1 Complex as a Calcium Sensor for Synaptic Vesicle Endocytosis*
Lai M, Hong J, Ruggiero A, Burnett P, Slepnev V, De Camilli P, Snyder S. The Calcineurin-Dynamin 1 Complex as a Calcium Sensor for Synaptic Vesicle Endocytosis*. Journal Of Biological Chemistry 1999, 274: 25963-25966. PMID: 10473536, DOI: 10.1074/jbc.274.37.25963.Peer-Reviewed Original ResearchConceptsCalcium sensorEndocytic coat proteinsSynaptic endocytic machinerySynaptic vesicle endocytosisSynaptic vesiclesCalcium-dependent phosphatase calcineurinEndocytic machineryVesicle endocytosisDynamin 1Phosphatase calcineurinCoat proteinCalcium-dependent formationCalcium-sensing mechanismPhysical associationEndocytosisVesiclesCalcium-dependent processesClathrinSynaptotagminComplexesExocytosisCalcineurinMachineryProteinEpidermal 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 geneGenesProliferation
1998
Phosphatidylinositol-4,5-bisphosphate is required for endocytic coated vesicle formation
Jost M, Simpson F, Kavran J, Lemmon M, Schmid S. Phosphatidylinositol-4,5-bisphosphate is required for endocytic coated vesicle formation. Current Biology 1998, 8: 1399-1404. PMID: 9889104, DOI: 10.1016/s0960-9822(98)00022-0.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex 2Adaptor Proteins, Vesicular TransportBiotinCell MembraneClathrinEndocytosisEndosomesHumansIsoenzymesMutagenesisNeomycinNerve Tissue ProteinsPhosphatidylinositol 4,5-DiphosphatePhospholipase C deltaPhosphoproteinsProtein BindingTransferrinTumor Cells, CulturedType C PhospholipasesConceptsCoated vesicle formationEndocytic coated vesicle formationVesicle formationPleckstrin homology domainClathrin-coated vesiclesInvolvement of phosphatidylinositolReceptor-mediated endocytosisBind phosphatidylinositolGTPase dynaminAP2 complexProtein playersEndocytic motifEndocytic machineryHomology domainPH domainCoat assemblyInositol polyphosphateHigh-specificity probesGTPase activityInositol lipidsPhosphatidylinositolFirst direct evidenceDirect evidenceClathrinEndocytosis
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