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
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
Frequent alterations in E-cadherin and alpha- and beta-catenin expression in human breast cancer cell lines.
Pierceall W, Woodard A, Morrow J, Rimm D, Fearon E. Frequent alterations in E-cadherin and alpha- and beta-catenin expression in human breast cancer cell lines. Oncogene 1995, 11: 1319-26. PMID: 7478552.Peer-Reviewed Original ResearchMeSH KeywordsAlpha CateninBase SequenceBeta CateninBlotting, SouthernBlotting, WesternBreast NeoplasmsCadherinsCytoskeletal ProteinsFemaleGene DeletionGene ExpressionHumansMolecular Sequence DataMutationOligodeoxyribonucleotidesPolymerase Chain ReactionPolymorphism, Single-Stranded ConformationalReceptor, ErbB-2RibonucleasesTrans-ActivatorsTumor Cells, CulturedConceptsAlpha-catenin proteinE-cadherin transcriptE-cadherinE-cadherin expressionBeta-catenin expressionCell linesBreast cancer cell linesEpithelial cell-cell interactionsCancer cell linesBeta-catenin proteinCancer-derived cell linesMembrane cytoskeletal proteinsCell-cell interactionsBreast cancer-derived cell linesE-cadherin geneHuman breast cancer-derived cell linesLoss of functionTransmembrane proteinAdherens junctionsCytoskeletal matrixCadherin proteinCytoskeletal proteinsTranscript levelsFrequent alterationsSequence alterations
1994
Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit.
Devarajan P, Scaramuzzino D, Morrow J. Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 2965-2969. PMID: 8159688, PMCID: PMC43495, DOI: 10.1073/pnas.91.8.2965.Peer-Reviewed Original ResearchConceptsK-ATPase alpha subunitMembrane transport proteinsCytoplasmic domainAlpha subunitK-ATPaseTransport proteinsIntegral membrane transport proteinsDomain IIPutative cytoplasmic domainInteraction of ankyrinDistinct cytoplasmic domainsATPase domainHuman erythrocyte spectrinSignificant homologyUbiquitous proteinSpectrin cytoskeletonRecombinant fusion proteinPrimary sequenceAnkyrinFusion proteinChannel proteinsClear functionSubunitsProteinSpectrin binds
1990
Radiolabel‐transfer cross‐linking demonstrates that protein 4.1 binds to the N‐terminal region of β spectrin and to actin in binary interactions
BECKER P, SCHWARTZ M, MORROW J, Samuel E. Radiolabel‐transfer cross‐linking demonstrates that protein 4.1 binds to the N‐terminal region of β spectrin and to actin in binary interactions. The FEBS Journal 1990, 193: 827-836. PMID: 2249696, DOI: 10.1111/j.1432-1033.1990.tb19406.x.Peer-Reviewed Original Research
1987
Characterization of intestinal brush border cytoskeletal proteins of normal and neoplastic human epithelial cells. A comparison with the avian brush border.
Carboni J, Howe C, West A, Barwick K, Mooseker M, Morrow J. Characterization of intestinal brush border cytoskeletal proteins of normal and neoplastic human epithelial cells. A comparison with the avian brush border. American Journal Of Pathology 1987, 129: 589-600. PMID: 3425692, PMCID: PMC1899811.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBirdsColonColonic NeoplasmsCytoskeletal ProteinsCytoskeletonEpithelial CellsEpitheliumHumansIleumImmunochemistryIntestinal MucosaIntestinesMicrovilliConceptsMicrovillar actin bundlesActin binding proteinsHuman brush borderIntestinal epithelial cell brush bordersEpithelial cell brush bordersBrush borderMicrovillar proteinsHuman epithelial cellsCytoskeletal matrixCytoskeletal proteinsMultiple proteinsActin bundlesImmunolocalization studiesSpectrin isoformsMammalian sourcesMajor proteinsDifferentiation stateBinding proteinProtein myosinProteinTerminal webCell brush borderCytoskeletonNeoplastic stateMature enterocytesAbnormal oxidant sensitivity and beta-chain structure of spectrin in hereditary spherocytosis associated with defective spectrin-protein 4.1 binding.
Becker P, Morrow J, Lux S. Abnormal oxidant sensitivity and beta-chain structure of spectrin in hereditary spherocytosis associated with defective spectrin-protein 4.1 binding. Journal Of Clinical Investigation 1987, 80: 557-565. PMID: 3611357, PMCID: PMC442269, DOI: 10.1172/jci113104.Peer-Reviewed Original ResearchThe interaction of calmodulin with human erythrocyte spectrin. Inhibition of protein 4.1-stimulated actin binding.
Anderson J, Morrow J. The interaction of calmodulin with human erythrocyte spectrin. Inhibition of protein 4.1-stimulated actin binding. Journal Of Biological Chemistry 1987, 262: 6365-6372. PMID: 3571263, DOI: 10.1016/s0021-9258(18)45579-2.Peer-Reviewed Original ResearchBeta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions.
Coleman T, Harris A, Mische S, Mooseker M, Morrow J. Beta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions. Journal Of Cell Biology 1987, 104: 519-526. PMID: 3818791, PMCID: PMC2114562, DOI: 10.1083/jcb.104.3.519.Peer-Reviewed Original Research
1986
Limited proteolysis of the erythrocyte membrane skeleton by calcium-dependent proteinases
Croall D, Morrow J, DeMartino G. Limited proteolysis of the erythrocyte membrane skeleton by calcium-dependent proteinases. Biochimica Et Biophysica Acta 1986, 882: 287-296. PMID: 3015225, DOI: 10.1016/0304-4165(86)90250-3.Peer-Reviewed Original Research
1984
Mechanisms of cytoskeletal regulation. Modulation of aortic endothelial cell spectrin by the extracellular matrix.
Pratt B, Harris A, Morrow J, Madri J. Mechanisms of cytoskeletal regulation. Modulation of aortic endothelial cell spectrin by the extracellular matrix. American Journal Of Pathology 1984, 117: 349-54. PMID: 6507585, PMCID: PMC1900592.Peer-Reviewed Original ResearchConceptsAortic endothelial cellsEndothelial cellsCultured aortic endothelial cellsSurface receptorsCalf aortic endothelial cellsVascular responsesExtracellular matrixVariety of stimuliPeripheral localizationWound repairReceptorsTransducers of informationMembrane receptorsCellsFibrillar formSpectrin distributionIntracellular distributionNonerythroid spectrinNeoplasiaInjuryFibronectin substrate