2007
Definition of a direct extracellular interaction between Met and E‐cadherin
Reshetnikova G, Troyanovsky S, Rimm DL. Definition of a direct extracellular interaction between Met and E‐cadherin. Cell Biology International 2007, 31: 366-373. PMID: 17336101, DOI: 10.1016/j.cellbi.2007.01.022.Peer-Reviewed Original ResearchConceptsBT-549 cellsE-cadherinCadherin-dependent cell-cell contactsHT-29 cellsE-cadherin interactsHepatocyte growth factorCell-cell adhesionCell-cell contactCross-linking studiesDirect extracellular interactionTyrosine kinase receptor expressionExtracellular interactionsMolecular mechanismsExtracellular domainIntracellular compartmentsPhysical interactionCellular presentationFirst evidenceGrowth factorCellsBT-549HT-29ExpressionReceptor expressionMetS
2006
Direct Interaction of the C-Terminal Domain of α-Catenin and F-Actin is Necessary for Stabilized Cell-Cell Adhesion
Pappas DJ, Rimm DL. Direct Interaction of the C-Terminal Domain of α-Catenin and F-Actin is Necessary for Stabilized Cell-Cell Adhesion. Cell Communication & Adhesion 2006, 13: 151-170. PMID: 16798615, DOI: 10.1080/15419060600726142.Peer-Reviewed Original ResearchConceptsF-actinF-actin interactionCell-cell adhesionC-terminal domainCell-cell contactFilamentous actin cytoskeletonActin cosedimentationActin cytoskeletonAdherens junctionsΑ-cateninColon carcinoma cell lineBasic residuesFusion proteinSingle residueAdhesive phenotypeDrop aggregationC-terminalAdhesive stateCarcinoma cell linesCharge mutationsDirect interactionIndirect binding mechanismsEpithelial monolayersCell linesBinding mechanism
2001
Truncated DCC Reduces N-Cadherin/Catenin Expression and Calcium-Dependent Cell Adhesion in Neuroblastoma Cells
Reyes-Múgica M, Meyerhardt J, Rzasa J, Rimm D, Johnson K, Wheelock M, Reale M. Truncated DCC Reduces N-Cadherin/Catenin Expression and Calcium-Dependent Cell Adhesion in Neuroblastoma Cells. Laboratory Investigation 2001, 81: 201-210. PMID: 11232642, DOI: 10.1038/labinvest.3780228.Peer-Reviewed Original ResearchMeSH KeywordsAlpha CateninBeta CateninCadherinsCalciumCell AdhesionCell Adhesion MoleculesCell AggregationColorectal NeoplasmsCytoskeletal ProteinsDCC ReceptorDesmogleinsDesmoplakinsGene Expression Regulation, NeoplasticGenes, DCCHumansNeuroblastomaReceptors, Cell SurfaceRecombinant ProteinsSequence DeletionTrans-ActivatorsTransfectionTumor Cells, CulturedTumor Suppressor ProteinsConceptsCalcium-dependent cell adhesionCell adhesionN-cadherinCell-cell contactCalcium-dependent aggregationCell aggregation studiesNorthern blot analysisNeuroblastoma cellsDCC proteinProtein functionNeural developmentFunctional linkColorectal cancer (DCC) proteinCellular migrationHuman neuroblastoma cell lineNeuroblastoma cell linesProteinBlot analysisCancer proteinsProtein levelsCell processesCell linesOverexpressionCatenin expressionDiminished expression
2000
α-Catenin Binds Directly to Spectrin and Facilitates Spectrin-Membrane Assembly in Vivo *
Pradhan D, Lombardo C, Roe S, Rimm D, Morrow J. α-Catenin Binds Directly to Spectrin and Facilitates Spectrin-Membrane Assembly in Vivo *. Journal Of Biological Chemistry 2000, 276: 4175-4181. PMID: 11069925, DOI: 10.1074/jbc.m009259200.Peer-Reviewed Original ResearchConceptsInteraction of spectrinClone A cellsΑ-catenin bindsAmino-terminal domainAmino acid regionSpectrin-actin skeletonCell-cell contactCell adhesion processesMadin-Darby canine kidneyAdhesion complexesConfluent Madin Darby canine kidneyCytoskeletal assemblyPlasma membraneDetergent solubilityMembrane assemblyAcid regionSpectrin skeletonMembrane regionsA cellsVivo roleSpectrinPhospholipid interactionsBiological membranesE-cadherinMolecular interactions
1999
PECAM-1 (CD31) functions as a reservoir for and a modulator of tyrosine-phosphorylated β-catenin
Ilan N, Mahooti S, Rimm D, Madri J. PECAM-1 (CD31) functions as a reservoir for and a modulator of tyrosine-phosphorylated β-catenin. Journal Of Cell Science 1999, 112: 3005-3014. PMID: 10462517, DOI: 10.1242/jcs.112.18.3005.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta CateninCattleCells, CulturedCytoskeletal ProteinsEndothelial Growth FactorsEndothelium, VascularGene ExpressionHumansIn Vitro TechniquesLymphokinesModels, BiologicalNeovascularization, PhysiologicPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Protein-Tyrosine KinasesTrans-ActivatorsTransfectionTyrosineVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsTyrosine phosphorylationBeta-catenin tyrosine phosphorylationBeta-catenin nuclear translocationAdherens junction formationProtein tyrosine kinasesPECAM-1 functionsTyrosine phosphorylation levelsCell-cell contactSW480 colon carcinoma cellsEndothelial cell-cell contactsCatenin functionVascular endothelial growth factorCell adhesion moleculeTranscriptional factorsPECAM-1Colon carcinoma cellsTyrosine kinaseGamma cateninMajor substrateJunctional proteinsCytoplasmic levelsPhosphorylation levelsNuclear translocationΒ-cateninCatenin
1995
Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex.
Rimm DL, Koslov ER, Kebriaei P, Cianci CD, Morrow JS. Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 8813-8817. PMID: 7568023, PMCID: PMC41057, DOI: 10.1073/pnas.92.19.8813.Peer-Reviewed Original ResearchConceptsF-actinBundling proteinE-cadherin-mediated cell-cell contactsHomotypic cell-cell adhesionBundles F-actinEpithelial cell polarityCortical actin cytoskeletonCell-cell adhesionActin-binding proteinsFull-length proteinE-cadherinCell-cell contactMembrane adhesion complexesBundles actinCell polarityHierarchy of interactionsActin cytoskeletonAdhesion complexesCytoplasmic domainCosedimentation assaysSedimentation assaysAdditional proteinsMolecular basisActin filamentsActin complexReceptor 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 activityCatenin