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 ResearchMeSH KeywordsAlpha CateninAnimalsBinding SitesCell LineCell MembraneCytoskeletal ProteinsDogsHumansProtein BindingSpectrinConceptsInteraction 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
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
The expression of p120ctn protein in breast cancer is independent of alpha- and beta-catenin and E-cadherin.
Dillon DA, D'Aquila T, Reynolds AB, Fearon ER, Rimm DL. The expression of p120ctn protein in breast cancer is independent of alpha- and beta-catenin and E-cadherin. American Journal Of Pathology 1998, 152: 75-82. PMID: 9422525, PMCID: PMC1858125.Peer-Reviewed Original ResearchA Mutation in α-Catenin Disrupts Adhesion in Clone A Cells Without Perturbing its Actin and β-Catenin Binding Activity
Roe S, Koslov E, Rimm D. A Mutation in α-Catenin Disrupts Adhesion in Clone A Cells Without Perturbing its Actin and β-Catenin Binding Activity. Cell Communication & Adhesion 1998, 5: 283-296. PMID: 9762469, DOI: 10.3109/15419069809040298.Peer-Reviewed Original ResearchMeSH KeywordsActinsAlpha CateninBeta CateninCadherinsCell AdhesionCloning, MolecularColonic NeoplasmsCytoskeletal ProteinsCytoskeletonDesmoplakinsExonsGamma CateninHeLa CellsHumansIntercellular JunctionsMutationOctoxynolPrecipitin TestsProtein BindingRecombinant Fusion ProteinsReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSequence Analysis, DNASolubilityTrans-ActivatorsTransfectionTumor Cells, CulturedConceptsN-terminusE-cadherin-catenin complexBundles F-actinCo-sedimentation assaysCell-cell adhesionFull-length proteinClone A cellsCo-precipitation experimentsInternal deletion mutationsWhole cell lysatesAdhesive complexesMutant proteinsA mutantsMutant bindsHuman colon carcinoma cell lineColon carcinoma cell lineMutant formsLength proteinWild typeCytoplasmic connectionsF-actinAdhesive phenotypeDeletion mutationsCell lysatesCarcinoma cell lines
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 lysatesα-Catenin Can Form Asymmetric Homodimeric Complexes and/or Heterodimeric Complexes with ॆ-Catenin*
Koslov E, Maupin P, Pradhan D, Morrow J, Rimm D. α-Catenin Can Form Asymmetric Homodimeric Complexes and/or Heterodimeric Complexes with ॆ-Catenin*. Journal Of Biological Chemistry 1997, 272: 27301-27306. PMID: 9341178, DOI: 10.1074/jbc.272.43.27301.Peer-Reviewed Original ResearchConceptsMembrane adhesion complexesHomodimeric complexCadherin moleculesAdhesion complexesAdhesive complexesHeterodimeric complexΑ-cateninOligomeric stateSurface plasmon resonance assaysMultimeric stateResidues 54Relative stoichiometryBiophysical techniquesMolecular massCell adhesionAmino acidsRecombinant moleculesHuman alphaRotary shadowingResonance assaysPrecise stoichiometryComplexesCytoskeletonCateninHomodimer
1995
Frequent alterations in E-cadherin and alpha- and beta-catenin expression in human breast cancer cell lines.
Pierceall W, Woodard A, Morrow J, Rimm D, Fearon E. Frequent alterations in E-cadherin and alpha- and beta-catenin expression in human breast cancer cell lines. Oncogene 1995, 11: 1319-26. PMID: 7478552.Peer-Reviewed Original ResearchMeSH KeywordsAlpha CateninBase SequenceBeta CateninBlotting, SouthernBlotting, WesternBreast NeoplasmsCadherinsCytoskeletal ProteinsFemaleGene DeletionGene ExpressionHumansMolecular Sequence DataMutationOligodeoxyribonucleotidesPolymerase Chain ReactionPolymorphism, Single-Stranded ConformationalReceptor, ErbB-2RibonucleasesTrans-ActivatorsTumor Cells, CulturedConceptsAlpha-catenin proteinE-cadherin transcriptE-cadherinE-cadherin expressionBeta-catenin expressionCell linesBreast cancer cell linesEpithelial cell-cell interactionsCancer cell linesBeta-catenin proteinCancer-derived cell linesMembrane cytoskeletal proteinsCell-cell interactionsBreast cancer-derived cell linesE-cadherin geneHuman breast cancer-derived cell linesLoss of functionTransmembrane proteinAdherens junctionsCytoskeletal matrixCadherin proteinCytoskeletal proteinsTranscript levelsFrequent alterationsSequence alterationsAlpha 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 activityCateninReduced alpha-catenin and E-cadherin expression in breast cancer.
Rimm DL, Sinard JH, Morrow JS. Reduced alpha-catenin and E-cadherin expression in breast cancer. Laboratory Investigation 1995, 72: 506-12. PMID: 7745946.Peer-Reviewed Original ResearchConceptsE-cadherinSteady-state levelsE-cadherin expressionHomotypic cell adhesion proteinMetastatic diseaseCell adhesion proteinsHuman E-cadherinCell-cell interactionsCytoplasmic proteinsTime of biopsyAdhesion proteinsAggressive tumor behaviorAdhesive functionEffector elementsAdhesion cascadeAbsent E-cadherin expressionTypes of cancerJunctional complexesProteinBreast cancerEpithelial tumorsSensitive markerTumor behaviorExpressionCancer
1994
Molecular Cloning Reveals Alternative Splice Forms of Human α(E)-Catenin
Rimm DL, Kebriaei P, Morrow JS. Molecular Cloning Reveals Alternative Splice Forms of Human α(E)-Catenin. Biochemical And Biophysical Research Communications 1994, 203: 1691-1699. PMID: 7945318, DOI: 10.1006/bbrc.1994.2381.Peer-Reviewed Original ResearchMeSH KeywordsAlpha CateninAlternative SplicingAmino Acid SequenceAnimalsBase SequenceCadherinsCell LineChickensCloning, MolecularConserved SequenceCytoskeletal ProteinsDNA, ComplementaryDrosophilaHominidaeHumansMiceMolecular Sequence DataPhylogenyPolymerase Chain ReactionRNA, MessengerSequence Homology, Amino AcidTranscription, GeneticConceptsCadherin cell-cell adhesion complexCell-cell adhesion complexAmino acid proteinAlternative splice formsSuperfamily of proteinsAmino acid insertionTranscription sitesAdhesion complexesCytoplasmic domainDistinct transcriptsMolecular cloningSingle geneAcid proteinSplice formsAcid insertionSecond transcriptCatenin geneSplice siteNon-epithelial tissuesVinculinTranscriptsCateninHuman alphaSouthern blottingProtein