2021
Deletion of Cdh16 Ksp-cadherin leads to a developmental delay in the ability to maximally concentrate urine in mouse
Thomson R, Dynia DW, Burlein S, Thomson BR, Booth C, Knauf F, Wang T, Aronson P. Deletion of Cdh16 Ksp-cadherin leads to a developmental delay in the ability to maximally concentrate urine in mouse. American Journal Of Physiology. Renal Physiology 2021, 320: f1106-f1122. PMID: 33938239, PMCID: PMC8285649, DOI: 10.1152/ajprenal.00556.2020.Peer-Reviewed Original ResearchConceptsKsp-cadherinCell adhesion moleculeAtypical memberKidney developmentMammalian kidneyAdult mammalian kidneyBasolateral membraneNormal kidney developmentEpithelial cellsAdhesion moleculesMutant animalsExpression analysisSpecific expressionE-cadherin expressionWestern blot analysisEpithelial phenotypePrincipal proteinE-cadherinBlot analysisMouse linesAquaporin-2CadherinCritical roleDevelopmental delayKnockout mice
2020
Fibronectin is a smart adhesive that both influences and responds to the mechanics of early spinal column development
Guillon E, Das D, Jülich D, Hassan AR, Geller H, Holley S. Fibronectin is a smart adhesive that both influences and responds to the mechanics of early spinal column development. ELife 2020, 9: e48964. PMID: 32228864, PMCID: PMC7108867, DOI: 10.7554/elife.48964.Peer-Reviewed Original ResearchConceptsNeural tubeParaxial mesodermZebrafish neural tubeNormal vertebrate developmentVertebrate trunkVertebrate developmentFibronectin remodelingFibronectin matrixConvergence defectsMorphogenesisExtracellular matrixMesodermFibronectinColumn developmentSmart adhesivesCadherinMutantsAdhesive lap jointsAdhesionLap jointsSymmetric interfacesRemodelingShear stressDefects
2019
Rhomboid-Like-2 Intramembrane Protease Mediates Metalloprotease-Independent Regulation of Cadherins
Battistini C, Rehman M, Avolio M, Arduin A, Valdembri D, Serini G, Tamagnone L. Rhomboid-Like-2 Intramembrane Protease Mediates Metalloprotease-Independent Regulation of Cadherins. International Journal Of Molecular Sciences 2019, 20: 5958. PMID: 31783481, PMCID: PMC6928865, DOI: 10.3390/ijms20235958.Peer-Reviewed Original ResearchConceptsE-cadherin extracellular domainIntramembrane proteasesExtracellular domainPost-translational regulationSame functional pathwayRhomboid familyRHBDL2Tissue homeostasisNovel regulatorCell motilityNegative regulatorFunctional pathwaysCadherinMajor familiesCell migrationAdhesive receptorsFunctional roleNovel mechanismVE-cadherinNovel MMPsE-cadherinCancer cellsRegulatorProteaseEndothelial cellsMitofusin 1 is required for female fertility and to maintain ovarian follicular reserve
Zhang M, Bener MB, Jiang Z, Wang T, Esencan E, Scott III R, Horvath T, Seli E. Mitofusin 1 is required for female fertility and to maintain ovarian follicular reserve. Cell Death & Disease 2019, 10: 560. PMID: 31332167, PMCID: PMC6646343, DOI: 10.1038/s41419-019-1799-3.Peer-Reviewed Original ResearchConceptsOocyte-granulosa cell communicationDynamic organellesAccumulation of ceramideFemale reproductive agingMitofusin 1Secondary follicle stageMitochondrial dynamicsCell communicationReproductive phenotypesCeramide synthesis inhibitor myriocinDevelopmental arrestApoptotic cell lossMitochondrial dysfunctionTargeted deletionOvarian follicular reserveOocyte maturationFemale fertilityFollicle stageDeletionPhenotypeReproductive agingOocytesCadherinFollicular reserveOrganelles
2012
Cadherin-based intercellular adhesions organize epithelial cell–matrix traction forces
Mertz AF, Che Y, Banerjee S, Goldstein JM, Rosowski KA, Revilla SF, Niessen CM, Marchetti MC, Dufresne ER, Horsley V. Cadherin-based intercellular adhesions organize epithelial cell–matrix traction forces. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 110: 842-847. PMID: 23277553, PMCID: PMC3549115, DOI: 10.1073/pnas.1217279110.Peer-Reviewed Original ResearchConceptsCell-cell adhesionExtracellular matrixIntercellular adhesionCell-matrix adhesionImportance of cadherinPrimary mouse keratinocytesTraction forceMechanical regulationFunction of tissuesCadherinColony peripheryCadherin expressionMinimal physical modelCross talkEssential roleMouse keratinocytesEpithelial tissuesEpithelial cellsContractile cellsPhysical cohesionSpatial rearrangementCellsColoniesAdhesionAdhesion typeApproaches in extracellular matrix engineering for determination of adhesion molecule mediated single cell function
Ayres-Sander C, Gonzalez A. Approaches in extracellular matrix engineering for determination of adhesion molecule mediated single cell function. Frontiers In Biology 2012, 8: 32-49. DOI: 10.1007/s11515-012-1199-x.Peer-Reviewed Original ResearchCell-ECM interactionsCell adhesion moleculeExtracellular matrixThree-dimensional matrixCellular processesNative extracellular matrixAdhesion moleculesTwo-dimensional substratesSingle cell functionCell functionCell movementECM proteinsNative proteinPeptide sequencesIntegrin expressionBioactive peptide sequencesCell functionalityMatrix engineeringProteinHuman tissuesCellsDiseased tissuesCadherinMoleculesTissueThe role and function of cadherins in the mammary gland
Andrews JL, Kim AC, Hens JR. The role and function of cadherins in the mammary gland. Breast Cancer Research 2012, 14: 203. PMID: 22315958, PMCID: PMC3496113, DOI: 10.1186/bcr3065.Peer-Reviewed Original ResearchConceptsMesenchymal-epithelial transitionEpithelial-mesenchymal transitionFunction of cadherinsMammary glandMechanism of regulationCell-cell contactPartial epithelial-mesenchymal transitionMetastatic cancer cellsLarge superfamilyNormal physiological conditionsTransmembrane receptorsCell motilityHeterophilic interactionsCadherinCadherin expressionCancer cellsMesenchymal markersPhysiological conditionsEpithelial cellsCurrent understandingRegulationMotilityDifferent organ systemsExpressionProliferation
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 moleculesCrosstalkAdhesion
2008
Cell adhesion receptors in mechanotransduction
Schwartz MA, DeSimone DW. Cell adhesion receptors in mechanotransduction. Current Opinion In Cell Biology 2008, 20: 551-556. PMID: 18583124, PMCID: PMC2581799, DOI: 10.1016/j.ceb.2008.05.005.Peer-Reviewed Original ResearchConceptsAdhesion receptorsCell fate decisionsCadherin-mediated adhesionCell adhesion receptorsFate decisionsMorphogenetic movementsTissue-level responsesCultured cellsExtracellular matrixMechanotransductionLevel responseCellsCytoskeletonCadherinReceptorsOrganismsAdhesionIntegrinsPathwayMechanical stimulationIntracellularMechanismMechanical stressResponseCentral mechanisms
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 moleculesCellsAdhesionFragmentsHomodimerHeterodimers
1999
Controversies at the cytoplasmic face of the cadherin-based adhesion complex
Provost E, Rimm D. Controversies at the cytoplasmic face of the cadherin-based adhesion complex. Current Opinion In Cell Biology 1999, 11: 567-572. PMID: 10508647, DOI: 10.1016/s0955-0674(99)00015-0.Peer-Reviewed Original ResearchMeSH Keywordsalpha CateninAnimalsArmadillo Domain Proteinsbeta CateninCadherinsCalciumCateninsCell AdhesionCell Adhesion MoleculesCytoplasmCytoskeletal ProteinsDelta CateninDimerizationDrosophila ProteinsHumansInsect ProteinsMacromolecular SubstancesMultigene FamilyPhosphoproteinsPhosphorylationProtein BindingProtein Processing, Post-TranslationalProtein Structure, TertiarySpectrinTrans-ActivatorsVinculin
1998
Dynamic Interaction of PTPμ with Multiple Cadherins In Vivo
Brady-Kalnay S, Mourton T, Nixon J, Pietz G, Kinch M, Chen H, Brackenbury R, Rimm D, Del Vecchio R, Tonks N. Dynamic Interaction of PTPμ with Multiple Cadherins In Vivo. Journal Of Cell Biology 1998, 141: 287-296. PMID: 9531566, PMCID: PMC2132733, DOI: 10.1083/jcb.141.1.287.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalCadherinsCell LineCell Line, TransformedCerebellumCross ReactionsElectrophoresis, Polyacrylamide GelHumansImmunoblottingMiceProtein Tyrosine PhosphatasesRatsReceptor-Like Protein Tyrosine Phosphatases, Class 2Receptor-Like Protein Tyrosine Phosphatases, Class 8Recombinant Fusion ProteinsRecombinant ProteinsSpodopteraTransfectionConceptsReversible tyrosine phosphorylationCadherin-catenin complexTyrosine phosphorylationE-cadherinWC5 cellsTemperature-sensitive mutant formPresence of cadherinCadherin functionV-SrcCytoplasmic segmentMultiple cadherinsCadherin-4PTPmuSf9 cellsMutant formsRegulatory mechanismsAdhesive functionCadherinN-cadherinPhosphorylationDirect interaction
1997
Vinculin Is Associated with the E-cadherin Adhesion Complex*
Hazan R, Kang L, Roe S, Borgen P, Rimm D. Vinculin Is Associated with the E-cadherin Adhesion Complex*. Journal Of Biological Chemistry 1997, 272: 32448-32453. PMID: 9405455, DOI: 10.1074/jbc.272.51.32448.Peer-Reviewed Original ResearchConceptsE-cadherin complexAdhesion complexesMDA-MB-468 cellsCalcium-dependent cell-cell adhesionE-cadherin adhesion complexAlpha-catenin geneCadherin-dependent adhesionCell-cell adhesionCell adhesion complexesE-cadherinCell linesAlpha-catenin expressionAlpha cateninReciprocal immunoprecipitationCytoplasmic interactionsCoprecipitation analysisAnti-vinculin antibodiesVinculinCadherinCytoplasmic connectionsFusion proteinE-cadherin expressionSame binding siteMDA-MB-468 breast cancer cell lineCell lysates
1996
Expression of a candidate cadherin in T lymphocytes.
Cepek KL, Rimm DL, Brenner MB. Expression of a candidate cadherin in T lymphocytes. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 6567-6571. PMID: 8692857, PMCID: PMC39065, DOI: 10.1073/pnas.93.13.6567.Peer-Reviewed Original ResearchConceptsCell adhesion eventsV8 protease digestionHuman T-cell leukemic cell lineT-cell leukemic cell lineCytoplasmic domainHomotypic adhesion moleculeCadherinLeukemic cell linesAdhesion eventsMolecular massProtease digestionHomotypic adhesionHeterotypic adhesionE-cadherinPeptide mapsSpeciesCell linesEpithelial cellsWider roleMucosal epithelial cellsAdhesion moleculesIntestinal intraepithelial T lymphocytesPan-cadherinCellsSolid tissues
1995
Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo.
Brady-Kalnay SM, Rimm DL, Tonks NK. Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo. Journal Of Cell Biology 1995, 130: 977-986. PMID: 7642713, PMCID: PMC2199947, DOI: 10.1083/jcb.130.4.977.Peer-Reviewed Original ResearchMeSH Keywordsalpha CateninAnimalsbeta CateninBinding SitesBrainCadherinsCell LineCytoskeletal ProteinsImmunoblottingImmunohistochemistryIntercellular JunctionsLungMembrane ProteinsMinkMyocardiumPhosphorylationPrecipitin TestsProtein BindingProtein Tyrosine PhosphatasesRatsReceptor-Like Protein Tyrosine Phosphatases, Class 2Receptor-Like Protein Tyrosine Phosphatases, Class 8Receptors, Cell SurfaceTissue DistributionTrans-ActivatorsVanadatesConceptsIntracellular segmentIntracellular domainCellular tyrosine phosphatase activityCadherin/catenin complexDynamic tyrosine phosphorylationImmunoglobulin domainFibronectin type III repeatsTyrosine phosphatase activityTyrosine-phosphorylated formType III repeatsCell-cell contactJuxtamembrane segmentPTP domainPervanadate treatmentMAM domainActin cytoskeletonCatenin complexPTPmuTyrosine phosphorylationExtracellular segmentCadherinEndogenous substratesMink lung cellsPhosphatase activityCateninIsolation and cDNA Cloning of Ksp-cadherin, a Novel Kidney-specific Member of the Cadherin Multigene Family *
Thomson R, Igarashi P, Biemesderfer D, Kim R, Abu-Alfa A, Soleimani M, Aronson P. Isolation and cDNA Cloning of Ksp-cadherin, a Novel Kidney-specific Member of the Cadherin Multigene Family *. Journal Of Biological Chemistry 1995, 270: 17594-17601. PMID: 7615566, DOI: 10.1074/jbc.270.29.17594.Peer-Reviewed Original ResearchConceptsKidney-specific memberMultigene familyKsp-cadherinCDNA cloningCharacteristic cysteine residuesT7 expression systemClassical cadherinsCytoplasmic domainCysteine residuesExpression systemTissue developmentImmunolocalization studiesRecognition sequenceNorthern analysisCadherinDemonstrated roleCellular recognitionMolecular analysisLI-cadherinHPT-1Basolateral membraneCloningRenal tubular epithelial cellsEpithelial cellsProtein
1994
Molecular Cloning of Human E-Cadherin Suggests a Novel Subdivision of the Cadherin Superfamily
Rimm DL, Morrow JS. Molecular Cloning of Human E-Cadherin Suggests a Novel Subdivision of the Cadherin Superfamily. Biochemical And Biophysical Research Communications 1994, 200: 1754-1761. PMID: 8185635, DOI: 10.1006/bbrc.1994.1656.Peer-Reviewed Original ResearchConceptsHuman E-cadherinClassical cadherinsE-cadherinDown-stream signaling cascadesCadherin functionRelated cadherinsHomology domainCytoplasmic domainSequence motifsDomain homologyUnprocessed proteinMolecular cloningCytoplasmic interactionsHuman proteinsCDNA libraryDesmosomal cadherinsSignaling cascadesCadherinMolecular massT-cadherinNovel subdivisionProteinRET oncogeneCloningHomology
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