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
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 Research
1997
α-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
Receptor 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
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