2020
In vitro physiological membrane‐on‐a‐chip and its application in cell and neuronal biology
Heo P, Rothman J, Pincet F. In vitro physiological membrane‐on‐a‐chip and its application in cell and neuronal biology. The FASEB Journal 2020, 34: 1-1. DOI: 10.1096/fasebj.2020.34.s1.08637.Peer-Reviewed Original ResearchNeuronal biologyTail-anchored proteinsPost-translational insertionMost biological processesAreas of biologyVesicle traffickingProtein insertionER membranePhysiological lipid compositionBiological processesMolecular mechanismsBiologyLipid compositionPhysiological membranesModel membranesMembraneInvaluable insightsCellsTraffickingProteinInsertionPatch-clamp amplifierΑ-synucleinopathiesCompositionBilayers
2014
CX3CL1, a chemokine finely tuned to adhesion: critical roles of the stalk glycosylation and the membrane domain
Ostuni M, Guellec J, Hermand P, Durand P, Combadière C, Pincet F, Deterre P. CX3CL1, a chemokine finely tuned to adhesion: critical roles of the stalk glycosylation and the membrane domain. Biology Open 2014, 3: 1173-1182. PMID: 25395671, PMCID: PMC4265755, DOI: 10.1242/bio.20149845.Peer-Reviewed Original ResearchCytosolic domainTransmembrane domainChemokine domainMucin stalkMembrane domainsHigh glycosylationFunctional rolePatrolling behaviorFunctional adhesion assaysAdhesion assaysCritical roleGlycosylationDomainCytoskeletonPermanent aggregationStructural analysisStalkAdhesionRoleMembraneCX3CL1CellsAssaysReceptors
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
Separation 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 moleculesCellsAdhesionFragmentsHomodimerHeterodimers