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
1998
Dynamic Interaction of PTPμ with Multiple Cadherins In Vivo
Brady-Kalnay S, Mourton T, Nixon J, Pietz G, Kinch M, Chen H, Brackenbury R, Rimm D, Del Vecchio R, Tonks N. Dynamic Interaction of PTPμ with Multiple Cadherins In Vivo. Journal Of Cell Biology 1998, 141: 287-296. PMID: 9531566, PMCID: PMC2132733, DOI: 10.1083/jcb.141.1.287.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalCadherinsCell LineCell Line, TransformedCerebellumCross ReactionsElectrophoresis, Polyacrylamide GelHumansImmunoblottingMiceProtein Tyrosine PhosphatasesRatsReceptor-Like Protein Tyrosine Phosphatases, Class 2Receptor-Like Protein Tyrosine Phosphatases, Class 8Recombinant Fusion ProteinsRecombinant ProteinsSpodopteraTransfectionConceptsReversible tyrosine phosphorylationCadherin-catenin complexTyrosine phosphorylationE-cadherinWC5 cellsTemperature-sensitive mutant formPresence of cadherinCadherin functionV-SrcCytoplasmic segmentMultiple cadherinsCadherin-4PTPmuSf9 cellsMutant formsRegulatory mechanismsAdhesive functionCadherinN-cadherinPhosphorylationDirect interactionA 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
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
1990
Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. I. High resolution epitope mapping and characterization of monoclonal antibody binding sites.
Rimm DL, Kaiser DA, Bhandari D, Maupin P, Kiehart DP, Pollard TD. Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. I. High resolution epitope mapping and characterization of monoclonal antibody binding sites. Journal Of Cell Biology 1990, 111: 2405-2416. PMID: 1703536, PMCID: PMC2116414, DOI: 10.1083/jcb.111.6.2405.Peer-Reviewed Original ResearchIdentification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions.
Sinard JH, Rimm DL, Pollard TD. Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions. Journal Of Cell Biology 1990, 111: 2417-2426. PMID: 2177477, PMCID: PMC2116375, DOI: 10.1083/jcb.111.6.2417.Peer-Reviewed Original ResearchMeSH KeywordsAcanthamoebaAnimalsBase SequenceBinding SitesChromatographyChromatography, DEAE-CelluloseChromatography, GelChromosome DeletionCloning, MolecularDurapatiteElectrophoresis, Polyacrylamide GelEscherichia coliHydroxyapatitesKineticsMacromolecular SubstancesMagnesiumMicroscopy, ElectronMolecular Sequence DataMolecular WeightMyosinsPotassium ChlorideRecombinant Fusion ProteinsScattering, RadiationConceptsFusion proteinMyosin IIMyosin-II tailAntiparallel tetramersAmino acidsAmino acid residuesNative myosin IIRecombinant fusion proteinSequence altersAcid residuesTail sequencesNH2-terminalNonhelical domainAcanthamoeba myosin IIFunctional regionsProteinParacrystal formationAntiparallel dimerAssembly propertiesDimerization mechanismResiduesTerminal deletionDeletionAssemblyTight packing
1989
New plasmid vectors for high level synthesis of eukaryotic fusion proteins in Escherichia coli
Rimm D, Pollard T. New plasmid vectors for high level synthesis of eukaryotic fusion proteins in Escherichia coli. Gene 1989, 75: 323-327. PMID: 2653968, DOI: 10.1016/0378-1119(89)90278-3.Peer-Reviewed Original ResearchConceptsFusion proteinBacterial proteinsPlasmid vectorEscherichia coliCloning sitePlasmid vector systemTotal soluble proteinEukaryotic fusion proteinsSoluble recombinant proteinInsertion of sequencesEukaryotic proteinsMultiple cloning sitePlasmid expression vectorTrpE proteinNew plasmid vectorRecombinant proteinsSoluble proteinExpression vectorTail sequencesAmino acidsProteinVector systemSequenceColiCell suspensions