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
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 stageSurvival
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
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
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