2020
CX3CL1 homo-oligomerization drives cell-to-cell adherence
Ostuni M, Hermand P, Saindoy E, Guillou N, Guellec J, Coens A, Hattab C, Desuzinges-Mandon E, Jawhari A, Iatmanen-Harbi S, Lequin O, Fuchs P, Lacapere J, Combadière C, Pincet F, Deterre P. CX3CL1 homo-oligomerization drives cell-to-cell adherence. Scientific Reports 2020, 10: 9069. PMID: 32494000, PMCID: PMC7271195, DOI: 10.1038/s41598-020-65988-w.Peer-Reviewed Original ResearchConceptsNumerous adhesion moleculesPhotobleaching assaysNative electrophoresisAdhesive potencyTransmembrane peptidesLipid environmentKey immune processesAdhesive functionFluorescence recoveryFunctional roleDomain peptideFluorescence kineticsOligomerizationCellular adherenceMolecular modelingAdhesion moleculesCell adherenceTransmembrane chemokineImmune processesCompact bundlePeptidesBlood leukocytesClustersElectrophoresisCX3CL1
2014
Arf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting
Wilfling F, Thiam AR, Olarte MJ, Wang J, Beck R, Gould TJ, Allgeyer ES, Pincet F, Bewersdorf J, Farese RV, Walther TC. Arf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting. ELife 2014, 3: e01607. PMID: 24497546, PMCID: PMC3913038, DOI: 10.7554/elife.01607.Peer-Reviewed Original ResearchMeSH KeywordsADP-Ribosylation Factor 1AnimalsBiological TransportCell LineCoat Protein Complex ICOP-Coated VesiclesDrosophila melanogasterDrosophila ProteinsEndoplasmic ReticulumHumansLipaseLipid DropletsLipolysisMiceNanoparticlesParticle SizePhospholipidsRNA InterferenceSurface TensionTime FactorsTransfectionTriglyceridesConceptsCellular lipid dropletsLipid dropletsProtein machineryProtein targetingUbiquitous organellesVesicle traffickingLD surfaceSpecific proteinsKey enzymeLD morphologyMembrane precursorsMachineryMetabolic energyProteinNeutral lipidsTG storageEnzymeUnclear mechanismsAmount of phospholipidsRecent evidenceOrganellesCOPITraffickingTriacylglycerolsBuds
2010
Integrins stimulate E-cadherin-mediated intercellular adhesion by regulating Src-kinase activation and actomyosin contractility
Martinez-Rico C, Pincet F, Thiery JP, Dufour S. Integrins stimulate E-cadherin-mediated intercellular adhesion by regulating Src-kinase activation and actomyosin contractility. Journal Of Cell Science 2010, 123: 712-722. PMID: 20144995, DOI: 10.1242/jcs.047878.Peer-Reviewed Original ResearchConceptsIntercellular adhesionActomyosin contractilityCell doubletsE-cadherin-mediated intercellular adhesionIntercellular adhesion strengthSrc family kinasesCell-matrix interactionsSrc kinase activationExistence of crosstalkRole of integrinsFamily kinasesCadherin-7Cell plasticityMolecular crosstalkMajor adhesion moleculeIntegrin stimulationCell spreadingCadherinCell adhesionII activityIntegrinsPolylysine-coated beadsAdhesion moleculesCrosstalkAdhesionThe adhesion mediated by the P-selectin P–selectin glycoprotein ligand-1 (PSGL-1) couple is stronger for shorter PSGL-1 variants
Barbaux S, Poirier O, Pincet F, Hermand P, Tiret L, Deterre P. The adhesion mediated by the P-selectin P–selectin glycoprotein ligand-1 (PSGL-1) couple is stronger for shorter PSGL-1 variants. Journal Of Leukocyte Biology 2010, 87: 727-734. PMID: 20051472, DOI: 10.1189/jlb.0609408.Peer-Reviewed Original Research
2008
Functional Adhesiveness of the CX3CL1 Chemokine Requires Its Aggregation ROLE OF THE TRANSMEMBRANE DOMAIN*
Hermand P, Pincet F, Carvalho S, Ansanay H, Trinquet E, Daoudi M, Combadière C, Deterre P. Functional Adhesiveness of the CX3CL1 Chemokine Requires Its Aggregation ROLE OF THE TRANSMEMBRANE DOMAIN*. Journal Of Biological Chemistry 2008, 283: 30225-30234. PMID: 18725411, PMCID: PMC2662081, DOI: 10.1074/jbc.m802638200.Peer-Reviewed Original ResearchConceptsBioluminescence resonance energy transferHomogeneous time-resolved fluorescenceTransmembrane domainAdhesive potencyTransmembrane domain residuesLoss of glycosylationConstitutive oligomersDomain residuesBRET signalTruncation experimentsResonance energy transferCell surfacePrimary cellsSpecific signalsNative formAdhesion assaysAdhesive moleculesCell linesCentral roleAggregation roleInhibition of CX3CL1New pathwayTime-resolved fluorescenceCellsAssays
2005
Prototypical Type I E-cadherin and Type II Cadherin-7 Mediate Very Distinct Adhesiveness through Their Extracellular Domains*
Chu YS, Eder O, Thomas WA, Simcha I, Pincet F, Ben-Ze'ev A, Perez E, Thiery JP, Dufour S. Prototypical Type I E-cadherin and Type II Cadherin-7 Mediate Very Distinct Adhesiveness through Their Extracellular Domains*. Journal Of Biological Chemistry 2005, 281: 2901-2910. PMID: 16253998, DOI: 10.1074/jbc.m506185200.Peer-Reviewed Original ResearchConceptsType II cadherinsE-cadherinIntercellular adhesivenessChimeric cadherinsTissue morphogenesisCadherin expression levelsCytoskeletal complexCytoplasmic tailCadherin-7Adherent junctionsCell doubletsCadherinExtracellular domainType ICell adhesivityExpression levelsStable complexesLow adhesivityCellsMorphogenesisAdhesivityComplexesProfound implicationsHigh adhesivityRegulation
2004
Force measurements in E-cadherin–mediated cell doublets reveal rapid adhesion strengthened by actin cytoskeleton remodeling through Rac and Cdc42
Chu Y, Thomas W, Eder O, Pincet F, Perez E, Thiery J, Dufour S. Force measurements in E-cadherin–mediated cell doublets reveal rapid adhesion strengthened by actin cytoskeleton remodeling through Rac and Cdc42. Journal Of Cell Biology 2004, 167: 1183-1194. PMID: 15596540, PMCID: PMC2172605, DOI: 10.1083/jcb.200403043.Peer-Reviewed Original ResearchConceptsActin cytoskeletonCadherin-dependent cell-cell adhesionE-cadherin-based adhesionsE-cadherin-expressing cellsCell adhesionActin cytoskeleton dynamicsRho-like small GTPasesCell-cell adhesionDominant active formDominant-negative formStrong cell adhesionFunctional cadherinCytoskeleton dynamicsSmall GTPasesCell doubletsHomophilic interactionsActin polymerizationIntercellular adhesionCdc42Negative formCadherinCell surfaceCadherin levelsCytoskeletonRacSeparation Force Measurements Reveal Different Types of Modulation of E-cadherin-based Adhesion by Nectin-1 and -3*
Martinez-Rico C, Pincet F, Perez E, Thiery J, Shimizu K, Takai Y, Dufour S. Separation Force Measurements Reveal Different Types of Modulation of E-cadherin-based Adhesion by Nectin-1 and -3*. Journal Of Biological Chemistry 2004, 280: 4753-4760. PMID: 15550395, DOI: 10.1074/jbc.m412544200.Peer-Reviewed Original ResearchConceptsE-cadherin-based adhesionsNectin-3E-cadherin-dependent cell adhesionExtracellular fragmentE-cadherin-mediated adhesionE-cadherin-expressing cellsNectin-1Cell adhesionCell-cell adhesionIndependent cell adhesion moleculesAdherens junctionsCell adhesion moleculeCell doubletsSignificant agonistic effectKey moleculesE-cadherinL cellsCadherinNectinAdhesion moleculesCellsAdhesionFragmentsHomodimerHeterodimersEnhanced Adhesive Capacities of the Naturally Occurring Ile249–Met280 Variant of the Chemokine Receptor CX3CR1*
Daoudi M, Lavergne E, Garin A, Tarantino N, Debré P, Pincet F, Combadière C, Deterre P. Enhanced Adhesive Capacities of the Naturally Occurring Ile249–Met280 Variant of the Chemokine Receptor CX3CR1*. Journal Of Biological Chemistry 2004, 279: 19649-19657. PMID: 14990582, DOI: 10.1074/jbc.m313457200.Peer-Reviewed Original Research