2005
β-Catenin Functions Mainly as an Adhesion Molecule in Patients with Squamous Cell Cancer of the Head and Neck
Yu Z, Weinberger PM, Provost E, Haffty BG, Sasaki C, Joe J, Camp RL, Rimm DL, Psyrri A. β-Catenin Functions Mainly as an Adhesion Molecule in Patients with Squamous Cell Cancer of the Head and Neck. Clinical Cancer Research 2005, 11: 2471-2477. PMID: 15814622, DOI: 10.1158/1078-0432.ccr-04-2199.Peer-Reviewed Original ResearchConceptsSquamous cell cancerCyclin D1 levelsCell cancerNeck squamous cell cancerAdhesion moleculesD1 levelsDisease-free survivalIndependent prognostic factorLocal recurrence rateKaplan-Meier analysisMembranous expression patternLow cyclin D1Cancer tissue microarrayIncidence of mutationsProtein expression levelsMean followHazard ratioPrognostic factorsLocal recurrencePathologic dataCox regressionRecurrence rateMetastasis stageTissue microarrayBeta-catenin expression
2004
Functional correlates of mutation of the Asp32 and Gly34 residues of beta-catenin
Provost E, McCabe A, Stern J, Lizardi I, D'Aquila TG, Rimm DL. Functional correlates of mutation of the Asp32 and Gly34 residues of beta-catenin. Oncogene 2004, 24: 2667-2676. PMID: 15829978, DOI: 10.1038/sj.onc.1208346.Peer-Reviewed Original ResearchConceptsThreonine residuesΒ-cateninStable MDCK cell linesCell linesCadherin-mediated adhesionMutant β-cateninMutant cell linesExon 3Stable cell linesDestruction motifKinase substrateTranscriptional activationUbiquitination statusMultifunctional proteinMDCK cell lineCellular transformationTarget genesKey serineFunctional implicationsTransforming propertiesMutationsResiduesMotifG34Ubiquitinationβ‐Catenin and p53 analyses of a breast carcinoma tissue microarray
Chung GG, Zerkowski MP, Ocal IT, Dolled‐Filhart M, Kang JY, Psyrri A, Camp RL, Rimm DL. β‐Catenin and p53 analyses of a breast carcinoma tissue microarray. Cancer 2004, 100: 2084-2092. PMID: 15139049, DOI: 10.1002/cncr.20232.Peer-Reviewed Original Research
2003
Functional Correlates of Mutations in β-Catenin Exon 3 Phosphorylation Sites*
Provost E, Yamamoto Y, Lizardi I, Stern J, D'Aquila TG, Gaynor RB, Rimm DL. Functional Correlates of Mutations in β-Catenin Exon 3 Phosphorylation Sites*. Journal Of Biological Chemistry 2003, 278: 31781-31789. PMID: 12799363, DOI: 10.1074/jbc.m304953200.Peer-Reviewed Original ResearchConceptsCasein kinase 1Mutation of serineGlycogen synthase kinase 3 betaSynthase kinase 3 betaMadin-Darby canine kidney cellsTarget genes cyclin D1Canine kidney cellsGene cyclin D1Threonine residuesPhosphorylation sitesDownstream genesStable transformationKinase activityWounding assayKinase 1Ser45Functional assaysThr41Functional differencesMutationsSoft agarExon 3Kidney cellsCyclin D1Ser33
2002
Tissue microarray‐based analysis shows phospho‐β‐catenin expression in malignant melanoma is associated with poor outcome
Kielhorn E, Provost E, Olsen D, D'Aquila TG, Smith BL, Camp RL, Rimm DL. Tissue microarray‐based analysis shows phospho‐β‐catenin expression in malignant melanoma is associated with poor outcome. International Journal Of Cancer 2002, 103: 652-656. PMID: 12494474, DOI: 10.1002/ijc.10893.Peer-Reviewed Original ResearchConceptsMalignant melanomaTissue microarray-based studyTissue microarray-based analysisWorse overall survivalDepth of invasionImmuno-histochemical analysisPhospho-specific antibodiesPhospho-β-catenin expressionOverall survivalMetastatic lesionsPrimary lesionPoor outcomePrognostic markerMelanomaUnique subsetNuclear stainingAntibodiesCatenin antibodyMicroarray-based analysisLesionsOutcomesCatenin expressionSer33/37/Thr41Microarray-based studiesHuman tissuesAutomated subcellular localization and quantification of protein expression in tissue microarrays
Camp RL, Chung GG, Rimm DL. Automated subcellular localization and quantification of protein expression in tissue microarrays. Nature Medicine 2002, 8: 1323-1328. PMID: 12389040, DOI: 10.1038/nm791.Peer-Reviewed Original ResearchMeSH KeywordsAlgorithmsBeta CateninCell CompartmentationCytoskeletal ProteinsNeoplasmsProteinsSubcellular FractionsTrans-ActivatorsConceptsSub-cellular localizationSubjective Differences in Outcome Are Seen as a Function of the Immunohistochemical Method Used on a Colorectal Cancer Tissue Microarray
Chung GG, Kielhorn EP, Rimm DL. Subjective Differences in Outcome Are Seen as a Function of the Immunohistochemical Method Used on a Colorectal Cancer Tissue Microarray. Clinical Colorectal Cancer 2002, 1: 237-242. PMID: 12450422, DOI: 10.3816/ccc.2002.n.005.Peer-Reviewed Original ResearchConceptsTissue microarrayTissue sectionsColorectal cancer tissue microarraySemiquantitative grading systemColorectal cancer specimensCancer tissue microarrayPatient outcomesLarge cohortSubjective assessmentCancer specimensImmunohistochemical methodsGrading systemNuclear stainingPathology literatureProtein expressionTissue samplesCell preparationsExpression levelsBeta-catenin antibodyCurrent standardImmunohistochemistryCohortOutcomesApparent increaseExpression
2001
Tissue microarray analysis of beta-catenin in colorectal cancer shows nuclear phospho-beta-catenin is associated with a better prognosis.
Chung GG, Provost E, Kielhorn EP, Charette LA, Smith BL, Rimm DL. Tissue microarray analysis of beta-catenin in colorectal cancer shows nuclear phospho-beta-catenin is associated with a better prognosis. Clinical Cancer Research 2001, 7: 4013-20. PMID: 11751495.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta CateninCadherinsCell LineCell NucleusColorectal NeoplasmsCytoplasmCytoskeletal ProteinsDogsGene Expression Regulation, NeoplasticHumansImmunohistochemistryNeoplasm StagingOligonucleotide Array Sequence AnalysisPhosphoproteinsPrognosisProportional Hazards ModelsRecombinant ProteinsReproducibility of ResultsSurvival RateTrans-ActivatorsTransfectionTreatment OutcomeConceptsOverall survivalNuclear expressionColorectal cancerSeries of patientsColorectal cancer specimensTissue microarray analysisMajority of cancersBetter prognosisClinical outcomesClinicopathological factorsImproved survivalCancer specimensTissue microarrayImmunohistochemical analysisMembranous stainingColorectal tumorigenesisCytoplasmic stainingMultivariate analysisSignificant associationCancerAdenomatous polyposis coli (APC) geneNuclear stainingBeta-catenin overexpressionOnly stageSurvivalβ-Catenin Dysregulation in Thyroid Neoplasms Down-Regulation, Aberrant Nuclear Expression, and CTNNB1 Exon 3 Mutations Are Markers for Aggressive Tumor Phenotypes and Poor Prognosis
Garcia-Rostan G, Camp R, Herrero A, Carcangiu M, Rimm D, Tallini G. β-Catenin Dysregulation in Thyroid Neoplasms Down-Regulation, Aberrant Nuclear Expression, and CTNNB1 Exon 3 Mutations Are Markers for Aggressive Tumor Phenotypes and Poor Prognosis. American Journal Of Pathology 2001, 158: 987-996. PMID: 11238046, PMCID: PMC1850336, DOI: 10.1016/s0002-9440(10)64045-x.Peer-Reviewed Original ResearchMeSH KeywordsAdenomaAdultAgedBeta CateninBiomarkers, TumorCarcinomaCell DivisionCell NucleusCytoskeletal ProteinsDown-RegulationExonsFemaleGene Expression Regulation, NeoplasticHumansMaleMiddle AgedOncogene Protein p21(ras)PhenotypePoint MutationPolymorphism, Single-Stranded ConformationalPrognosisSurvival RateThyroid NeoplasmsTrans-ActivatorsConceptsPoor prognosisTumor differentiationBeta-catenin expressionConventional prognostic indicatorsAggressive tumor phenotypeNuclear beta-catenin localizationThyroid tumor samplesBeta-catenin dysregulationAberrant nuclear expressionΒ-catenin dysregulationDifferentiated tumorsPrognostic indicatorThyroid cancerThyroid neoplasmsNuclear immunoreactivityBeta-catenin alterationsNuclear expressionTumor samplesProgressive lossCarcinomaTumor phenotypeSingle-strand conformational polymorphismBeta-catenin mutationsHuman cancersDown regulationParathyroid hormone-related protein maintains mammary epithelial fate and triggers nipple skin differentiation during embryonic breast development
Foley J, Dann P, Hong J, Cosgrove J, Dreyer B, Rimm D, Dunbar M, Philbrick W, Wysolmerski J. Parathyroid hormone-related protein maintains mammary epithelial fate and triggers nipple skin differentiation during embryonic breast development. Development 2001, 128: 513-525. PMID: 11171335, DOI: 10.1242/dev.128.4.513.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta CateninCell DifferentiationCell LineageCytoskeletal ProteinsDNA-Binding ProteinsEpidermal CellsEpidermisEpithelial CellsFemaleGene Expression Regulation, DevelopmentalHistocytochemistryLymphoid Enhancer-Binding Factor 1Mammary Glands, AnimalMiceMice, KnockoutMice, TransgenicModels, BiologicalNipplesParathyroid Hormone-Related ProteinProteinsReceptor, Parathyroid Hormone, Type 1Receptors, Parathyroid HormoneSignal TransductionTrans-ActivatorsTranscription FactorsTransgenesConceptsPTH/PTHrP receptorCell fateHormone-related proteinMammary epithelial cell fateMammary mesenchymeCell fate decisionsEpithelial cell fatePTHrP receptorEmbryonic mammary glandMesenchymal cellsType I PTH/PTHrP receptorEmbryonic mammary developmentMammary epithelial cellsParathyroid hormone-related proteinEpithelial cellsEpithelial fateEpidermal fateFate decisionsEpithelial morphogenesisAbsence of PTHrPMesenchymal expressionVentral epidermisProper developmentSkin differentiationCombination of lossTruncated 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-ActivatorsVinculinPECAM-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-cateninCateninBeta- and gamma-catenin mutations, but not E-cadherin inactivation, underlie T-cell factor/lymphoid enhancer factor transcriptional deregulation in gastric and pancreatic cancer.
Caca K, Kolligs FT, Ji X, Hayes M, Qian J, Yahanda A, Rimm DL, Costa J, Fearon ER. Beta- and gamma-catenin mutations, but not E-cadherin inactivation, underlie T-cell factor/lymphoid enhancer factor transcriptional deregulation in gastric and pancreatic cancer. Molecular Cancer Research 1999, 10: 369-76. PMID: 10392898.Peer-Reviewed Original ResearchMeSH KeywordsAdenomatous Polyposis Coli ProteinAmino Acid SequenceAnimalsBeta CateninCadherinsCytoskeletal ProteinsDesmoplakinsDNA-Binding ProteinsGamma CateninGene Expression Regulation, NeoplasticHMGB ProteinsHumansLymphoid Enhancer-Binding Factor 1Molecular Sequence DataMutagenesisPancreatic NeoplasmsStomach NeoplasmsTCF Transcription FactorsTrans-ActivatorsTranscription Factor 7-Like 1 ProteinTranscription FactorsTranscription, GeneticTumor Cells, CulturedConceptsPhosphorylation sitesMutant proteinsGlycogen synthase kinase 3beta phosphorylation sitesGlycogen synthase kinase-3betaFactor transcription factorsPotential phosphorylation sitesSynthase kinase-3betaTCF transcriptional activityE-cadherin inactivationNH2-terminal deletionsRole of APCImportant binding partnerSerine 28TCF transcriptionTranscriptional deregulationT-cell factorBinding partnerTranscription factorsAPC proteinKinase-3betaTranscriptional activityNH2 terminusAdenomatous polyposis coli (APC) mutationsCell adhesionPancreatic cancer linesFrequent 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
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 lysates