2008
Prognostic Significance of Cadherin-Based Adhesion Molecules in Cutaneous Malignant Melanoma
Kreizenbeck GM, Berger AJ, Subtil A, Rimm DL, Rothberg BE. Prognostic Significance of Cadherin-Based Adhesion Molecules in Cutaneous Malignant Melanoma. Cancer Epidemiology Biomarkers & Prevention 2008, 17: 949-958. PMID: 18398036, PMCID: PMC3312613, DOI: 10.1158/1055-9965.epi-07-2729.Peer-Reviewed Original Research
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
1999
Frequent mutation and nuclear localization of beta-catenin in anaplastic thyroid carcinoma.
Garcia-Rostan G, Tallini G, Herrero A, D'Aquila TG, Carcangiu ML, Rimm DL. Frequent mutation and nuclear localization of beta-catenin in anaplastic thyroid carcinoma. Cancer Research 1999, 59: 1811-5. PMID: 10213482.Peer-Reviewed Original ResearchConceptsNuclear localizationSingle-strand conformational polymorphismE-cadherin-mediated cell-cell adhesionBeta-catenin actsFrequent nuclear localizationCell-cell adhesionExon 3Conformational polymorphismBeta-catenin genePhosphorylation sitesWingless pathwayTranscriptional activationCytoplasmic proteinsSubcellular localizationMobility shiftMutational analysisNucleotide sequencingDNA sequencingNuclear translocationSomatic alterationsMutationsAnaplastic thyroid carcinomaSequencingProteinFrequent mutationsFrequent Nuclear/Cytoplasmic Localization of β-Catenin without Exon 3 Mutations in Malignant Melanoma
Rimm D, Caca K, Hu G, Harrison F, Fearon E. Frequent Nuclear/Cytoplasmic Localization of β-Catenin without Exon 3 Mutations in Malignant Melanoma. American Journal Of Pathology 1999, 154: 325-329. PMID: 10027390, PMCID: PMC1850000, DOI: 10.1016/s0002-9440(10)65278-9.Peer-Reviewed Original ResearchConceptsCytoplasmic localizationPhosphorylation sitesE-cadherin-mediated cell-cell adhesionGlycogen synthase kinase 3beta phosphorylation sitesMelanoma cell linesN-terminal phosphorylation sitesWnt pathwayExon 3 mutationsCell linesGlycogen synthase kinase-3betaFactor transcription factorsBeta-catenin accumulatesCell-cell adhesionSynthase kinase-3betaBeta-catenin exon 3 mutationsDNA sequencing studiesAdenomatous polyposis coliAxin proteinTranscription factorsKinase-3betaAmino terminusBeta-CateninBeta-catenin mutationsWnt pathway activationSequencing studies
1998
A 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 lysates
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 complex