2001
Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain
Zhang Z, Weed S, Gallagher P, Morrow J. Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain. Blood 2001, 98: 1645-1653. PMID: 11535493, DOI: 10.1182/blood.v98.6.1645.Peer-Reviewed Original ResearchConceptsSelf-association domainPoint mutationsHuman sequenceDrosophila alpha-spectrinDynamic molecular modelingHuman erythrocyte spectrinCytoskeletal functionSpecific point mutationsConservative substitutionsPrimary sequenceConformational rearrangementsAlpha-spectrinHelical regionHydrophilic residuesAmino acidsMutationsSpectrinSalt bridgeErythrocyte spectrinStructural consequencesPathogenic mutationsRepeat unitsMolecular modelingSequenceStructural disruptionCaspase Remodeling of the Spectrin Membrane Skeleton during Lens Development and Aging*
Lee A, Morrow J, Fowler V. Caspase Remodeling of the Spectrin Membrane Skeleton during Lens Development and Aging*. Journal Of Biological Chemistry 2001, 276: 20735-20742. PMID: 11278555, DOI: 10.1074/jbc.m009723200.Peer-Reviewed Original ResearchMeSH KeywordsAgingAmino Acid SequenceAnimalsBase SequenceCaspasesCell MembraneChickensDNA PrimersLens, CrystallineMolecular Sequence DataRatsSpectrinConceptsLens fiber cellsFiber cellsMembrane blebbingMembrane skeletonLens developmentAlpha-spectrinSpectrin membrane skeletonMembrane skeleton componentsChick lens developmentCell-cell fusionApoptotic cellsOldest fiber cellsMembrane associationClassical apoptosisApoptotic processSpecific proteolysisTerminal differentiationAdult lensSpectrin fragmentsMembrane interdigitationsBlebbingCytoskeletal protein alpha-spectrinPermanent remodelingSkeleton componentsSpectrin
2000
Identification and Characterization of βV Spectrin, a Mammalian Ortholog of Drosophila βHSpectrin* 210
Stabach P, Morrow J. Identification and Characterization of βV Spectrin, a Mammalian Ortholog of Drosophila βHSpectrin* 210. Journal Of Biological Chemistry 2000, 275: 21385-21395. PMID: 10764729, DOI: 10.1074/jbc.c000159200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansCloning, MolecularConsensus SequenceDNA, ComplementaryDrosophilaDrosophila ProteinsExonsGene LibraryHumansIntronsMammalsMolecular Sequence DataMolecular WeightOrgan SpecificityPhylogenyRatsRecombinant ProteinsRepetitive Sequences, Amino AcidRetinaSequence AlignmentSequence Homology, Amino AcidSpectrinTumor Cells, CulturedViral ProteinsConceptsDrosophila orthologMammalian orthologsSpectrin repeatsPleckstrin homology domainComplete cDNA sequenceActin-binding domainSelf-association domainAmino acids 85Amino acid sequenceBeta-spectrin geneHuman retina cDNA libraryRetina cDNA libraryFly counterpartMammalian spectrinsCaenorhabditis elegansHomology domainEpithelial cell populationsSH3 domainApical domainCDNA sequenceCDNA libraryOrthologsPolarized epitheliumBeta spectrinAcid sequenceIdentification and Characterization of Human SLP-2, a Novel Homologue of Stomatin (Band 7.2b) Present in Erythrocytes and Other Tissues*
Wang Y, Morrow J. Identification and Characterization of Human SLP-2, a Novel Homologue of Stomatin (Band 7.2b) Present in Erythrocytes and Other Tissues*. Journal Of Biological Chemistry 2000, 275: 8062-8071. PMID: 10713127, DOI: 10.1074/jbc.275.11.8062.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntibody SpecificityBlood ProteinsCloning, MolecularCytoskeletonDNA, ComplementaryErythrocyte MembraneHumansMembrane ProteinsMolecular Sequence DataMultigene FamilyNerve Tissue ProteinsProtein BindingProtein BiosynthesisProtein Structure, TertiarySequence Analysis, DNASequence Analysis, ProteinSequence Homology, Amino AcidTissue DistributionConceptsIntegral membrane proteinsMembrane proteinsStomatin homologueSLP-1SLP-2Human stomatinCholesterol-rich lipid raftsLipid domain organizationTerminal hydrophobic domainAmino acid sequenceCultured COS cellsMature human erythrocytesSDS-polyacrylamide gel electrophoresis analysisErythrocyte membrane proteinsDomain organizationNonerythroid tissuesLipid raftsStomatin genePeripheral cytoskeletonChromosome 9p13StomatinAcid sequenceGel electrophoresis analysisCOS cellsRelated proteins
1999
Brain and Muscle Express a Unique Alternative Transcript of αΙΙ Spectrin †
Cianci C, Zhang Z, Pradhan D, Morrow J. Brain and Muscle Express a Unique Alternative Transcript of αΙΙ Spectrin †. Biochemistry 1999, 38: 15721-15730. PMID: 10625438, DOI: 10.1021/bi991458k.Peer-Reviewed Original ResearchConceptsAlternative mRNA splicingMRNA splicingAlphaII-spectrinBp insertionNovel protein interaction siteEmbryonic tissuesInsert 2Alternative exon usageProtein interaction sitesAmino acid sequenceDifferent splice formsAmino acid insertionMouse embryonic tissuesInsert-1Amino acid substitutionsSkeletal muscleGene familyDynamic molecular modelingMature proteinUnanticipated functionAlternative splicingExon usageIndividual transcriptsAlternative transcriptsSplice forms
1998
Structure of the Ankyrin-binding Domain of α-Na,K-ATPase*
Zhang Z, Devarajan P, Dorfman A, Morrow J. Structure of the Ankyrin-binding Domain of α-Na,K-ATPase*. Journal Of Biological Chemistry 1998, 273: 18681-18684. PMID: 9668035, DOI: 10.1074/jbc.273.30.18681.Peer-Reviewed Original ResearchConceptsK-ATPaseUbiquitous membrane proteinsSecond cytoplasmic domainSpecific macromolecular interactionsMadin-Darby canine kidney cellsAlpha-NACanine kidney cellsCytoplasmic domainThree-dimensional structureMembrane proteinsGlutathione S-transferasePlasma membraneRegulatory proteinsAnkyrinAmino acids bindFusion proteinResidues 142Trisphosphate receptorVectorial transportSurface loopsMacromolecular interactionsMultiple ankyrinHydrophilic faceS-transferaseFusion peptideUtilization of an 86bp exon generates a novel adducin isoform (β4) lacking the MARCKS homology domain1The first two authors contributed equally to this work.1
Sinard J, Stewart G, Stabach P, Argent A, Gilligan D, Morrow J. Utilization of an 86bp exon generates a novel adducin isoform (β4) lacking the MARCKS homology domain1The first two authors contributed equally to this work.1. Biochimica Et Biophysica Acta 1998, 1396: 57-66. PMID: 9524222, DOI: 10.1016/s0167-4781(97)00167-x.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceBase SequenceCalmodulin-Binding ProteinsCloning, MolecularExonsHumansIntracellular Signaling Peptides and ProteinsIsomerismMembrane ProteinsMolecular Sequence DataMyristoylated Alanine-Rich C Kinase SubstrateOrgan SpecificityPolymerase Chain ReactionProtein Structure, TertiaryProteinsSequence Homology, Amino AcidSequence Homology, Nucleic AcidTranscription, GeneticConceptsNovel amino acidAmino acidsBeta-adducinNew isoformHuman bone marrow cDNA libraryBone marrow cDNA libraryDifferent reading framesCalcium/calmodulinLysine-rich sequenceNT-2 cellsProtein kinase CGenomic clonesGenomic mapNew amino acidsAlternate exonsActin crossCDNA libraryReading frameSplice consensus sequenceNew exonsNovel isoformConsensus sequenceStop codonKinase CExons
1997
Site-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †
Stabach P, Cianci C, Glantz S, Zhang Z, Morrow J. Site-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †. Biochemistry 1997, 36: 57-65. PMID: 8993318, DOI: 10.1021/bi962034i.Peer-Reviewed Original ResearchConceptsSite-directed mutagenesisAlpha II spectrinCalpain cleavage sitesCleavage siteII-spectrinHelix CRecombinant GST-fusion proteinsBona fide proteinGST fusion proteinTriple-helical motifsStrict substrate specificityFamily of Ca2Protein kinase CDynamic molecular modelingStructural repeatsProminent substrateDifferent amino acidsSubstrate specificityIntracellular proteolysisPenultimate residueCysteine proteasesKinase CMost proteasesSteroid receptor activationSpectrin
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
Beta II-spectrin (fodrin) and beta I epsilon 2-spectrin (muscle) contain NH2- and COOH-terminal membrane association domains (MAD1 and MAD2).
Lombardo C, Weed S, Kennedy S, Forget B, Morrow J. Beta II-spectrin (fodrin) and beta I epsilon 2-spectrin (muscle) contain NH2- and COOH-terminal membrane association domains (MAD1 and MAD2). Journal Of Biological Chemistry 1994, 269: 29212-29219. PMID: 7961888, DOI: 10.1016/s0021-9258(19)62032-6.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainBeta II spectrinHomology domainSequence motifsBeta III-spectrinBrain spectrinGlutathione S-transferase fusion proteinRepeat 1S-transferase fusion proteinMembrane association domainNovel functional motifsCOOH-terminal domainG protein bindingDistinct sequence motifsBovine brain spectrinCOOH-terminal sequenceAssociation domainMembrane associationProtein 4.1Spectrin functionSequence comparisonPlasma membraneFunctional motifsRecombinant proteinsAnkyrin 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 bindsA partial structural repeat forms the heterodimer self-association site of all beta-spectrins
Kennedy S, Weed S, Forget B, Morrow J. A partial structural repeat forms the heterodimer self-association site of all beta-spectrins. Journal Of Biological Chemistry 1994, 269: 11400-11408. PMID: 8157672, DOI: 10.1016/s0021-9258(19)78138-1.Peer-Reviewed Original ResearchAmino Acid SequenceBase SequenceBinding SitesCloning, MolecularDNA PrimersErythrocytesEscherichia coliGlutathione TransferaseHumansKineticsMacromolecular SubstancesModels, StructuralMolecular Sequence DataProtein Structure, SecondaryRecombinant Fusion ProteinsRecombinant ProteinsRepetitive Sequences, Nucleic AcidSpectrin
1993
The 270 kDa splice variant of erythrocyte beta-spectrin (beta I sigma 2) segregates in vivo and in vitro to specific domains of cerebellar neurons.
Malchiodi-Albedi F, Ceccarini M, Winkelmann J, Morrow J, Petrucci T. The 270 kDa splice variant of erythrocyte beta-spectrin (beta I sigma 2) segregates in vivo and in vitro to specific domains of cerebellar neurons. Journal Of Cell Science 1993, 106 ( Pt 1): 67-78. PMID: 8270644, DOI: 10.1242/jcs.106.1.67.Peer-Reviewed Original ResearchConceptsBeta IPostsynaptic densityMultiple alternative transcriptsBeta-spectrin isoformBeta-spectrin genePlasma membrane stainingAlpha beta heterodimersNon-erythroid alpha-spectrinRegion of alphaCerebellar granule cellsDistinct genesPrecise segregationSubstantial homologyBiochemical restrictionsSingle protein bandAlternative transcriptsDistinct cytoplasmicUnique sequencesCerebellar neuronsSpectrin isoformsBeta heterodimerAlpha-spectrinSpectrin complexSplice variantsTargeting mechanismCloning of a Portion of the Chromosomal Gene and cDNA for Human β-Fodrin, the Nonerythroid Form of β-Spectrin
Chang J, Scarpa A, Eddy R, Byers M, Harris A, Morrow J, Watkins P, Shows T, Forget B. Cloning of a Portion of the Chromosomal Gene and cDNA for Human β-Fodrin, the Nonerythroid Form of β-Spectrin. Genomics 1993, 17: 287-293. PMID: 8406479, DOI: 10.1006/geno.1993.1323.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBrainCarrier ProteinsChromosome MappingChromosomes, Human, Pair 2Cloning, MolecularDNA ProbesDNA, ComplementaryExonsHumansHybrid CellsIntronsMiceMicrofilament ProteinsMolecular Sequence DataNerve Tissue ProteinsOligonucleotide ProbesRestriction MappingSequence Homology, Amino AcidSpectrinConceptsAmino acid sequenceAcid sequenceNonerythroid formsDNA sequencesSimilar exon/intron organizationGenomic DNAExon/intron organizationSomatic hybrid cell linesCell cDNA libraryHuman genomic librarySingle-copy DNA fragmentsSingle-copy probesComposite DNA sequenceDNA sequence analysisHybrid cell linesIntron organizationChromosomal localizationGenomic clonesGenomic libraryGenomic fragmentChromosomal genesCDNA clonesCDNA libraryChromosome 2Nucleotide sequenceCalmodulin-binding domain of recombinant erythrocyte beta-adducin.
Scaramuzzino D, Morrow J. Calmodulin-binding domain of recombinant erythrocyte beta-adducin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 3398-3402. PMID: 8475088, PMCID: PMC46307, DOI: 10.1073/pnas.90.8.3398.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBinding SitesBlood ProteinsCalmodulinCalmodulin-Binding ProteinsCalpainCattleCloning, MolecularDNAErythrocytesKineticsMacromolecular SubstancesMolecular Sequence DataOligodeoxyribonucleotidesPhosphorylationProtein Structure, SecondaryRecombinant ProteinsRestriction MappingTrypsinConceptsCaM-binding activityBeta-adducinBundles F-actinProtease-sensitive domainsCAMP-dependent kinaseCaM-binding domainPartial cDNA cloneBinding of spectrinAmino acid codeDependent CaM bindingProtein kinase CSingle letter amino acid codeCaM-binding sequenceProtease-resistant corePEST sequenceCovalent phosphorylationShares structural featuresCDNA clonesCortical cytoskeletonHeterodimeric proteinStructural basisConsensus sequenceMammalian erythrocytesProtease sensitivityBind calmodulin
1992
Karyoplasmic interaction selection strategy: a general strategy to detect protein-protein interactions in mammalian cells.
Fearon E, Finkel T, Gillison M, Kennedy S, Casella J, Tomaselli G, Morrow J, Van Dang C. Karyoplasmic interaction selection strategy: a general strategy to detect protein-protein interactions in mammalian cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 7958-7962. PMID: 1387709, PMCID: PMC49834, DOI: 10.1073/pnas.89.17.7958.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCHO CellsCricetinaeCytoplasmDNA-Binding ProteinsFlow CytometryFungal ProteinsHerpes Simplex Virus Protein Vmw65Hybrid CellsMacromolecular SubstancesMolecular Sequence DataProtein BindingRecombinant ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsTransfectionViral ProteinsConceptsProtein-protein interactionsMammalian cellsChimeric proteinReporter geneYeast transcriptional activator GAL4KISS systemSpecific protein-protein interactionsTranscriptional activator GAL4Transcriptional activation domainNovel protein interactionsDNA-binding domainTranscriptional activation functionSpecific interactionsActivator GAL4Activation domainProtein interactionsResultant transcriptionCDNA librarySelectable markerGAL4Drug resistance markersCell surfaceProteinTranscriptionGenes
1991
Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin.
Kennedy S, Warren S, Forget B, Morrow J. Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin. Journal Of Cell Biology 1991, 115: 267-277. PMID: 1833409, PMCID: PMC2289929, DOI: 10.1083/jcb.115.1.267.Peer-Reviewed Original ResearchConceptsAmino-terminal halfRepeat unitsCarboxy-terminal halfCOOH-terminal thirdProkaryotic expression systemNonerythroid cellsIntegral proteinsErythrocyte membrane vesiclesBeta spectrinResidue segmentExpression systemAnkyrinNuclease digestionNonhomologous segmentsMembrane vesiclesTerminal thirdAttachment of spectrinNative spectrinSpectrinAmino acidsPosition 45RepeatsSedimentation velocity experimentsRepetitive unitsCDNA
1988
Comparison of nonerythroid alpha-spectrin genes reveals strict homology among diverse species.
Leto T, Fortugno-Erikson D, Barton D, Yang-Feng T, Francke U, Harris A, Morrow J, Marchesi V, Benz E. Comparison of nonerythroid alpha-spectrin genes reveals strict homology among diverse species. Molecular And Cellular Biology 1988, 8: 1-9. PMID: 3336352, PMCID: PMC363070, DOI: 10.1128/mcb.8.1.1.Peer-Reviewed Original ResearchConceptsAlpha-spectrin geneErythroid alpha-spectrin geneHuman chromosome 9Alpha-spectrin chainComparison of sequencesCarboxy-terminal sequenceErythroid genesDiverse speciesExpression libraryChromosome 1Hydrophobic residuesErythroid spectrinAlpha-spectrinFilamentous proteinsFunctional sitesGenesChromosome 9Human cloneStrict homologyRepeat patternCell membraneInvariant tryptophanSpectrinPeptide sequencesCDNA