2001
βIII Spectrin Binds to the Arp1 Subunit of Dynactin*
Holleran E, Ligon L, Tokito M, Stankewich M, Morrow J, Holzbaur E. βIII Spectrin Binds to the Arp1 Subunit of Dynactin*. Journal Of Biological Chemistry 2001, 276: 36598-36605. PMID: 11461920, DOI: 10.1074/jbc.m104838200.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBinding SitesBrainCell MembraneCOS CellsCytoplasmCytosolDynactin ComplexElectrophoresis, Polyacrylamide GelGlutathione TransferaseImmunoblottingImmunohistochemistryMicrofilament ProteinsMicrotubule-Associated ProteinsPrecipitin TestsProtein BindingProtein IsoformsProtein Structure, TertiaryRatsSpectrinSrc Homology DomainsTwo-Hybrid System TechniquesConceptsBetaIII spectrinGolgi vesicle traffickingMicrotubule motor complexAssociation of dyneinVesicle traffickingVesicular cargoRat brain cytosolMitotic spindleIntracellular motorsCytoplasmic dyneinCleavage furrowDynactinInterphase cellsArp1Spectrin isoformsCytoplasmic vesiclesF-actinActin bindsEndoplasmic reticulumPerinuclear regionNovel localizationSpectrinDyneinBrain cytosolΒIII spectrinSpectrin Oligomerization is Cooperatively Coupled to Membrane Assembly: A Linkage Targeted by Many Hereditary Hemolytic Anemias?
Giorgi M, Cianci C, Gallagher P, Morrow J. Spectrin Oligomerization is Cooperatively Coupled to Membrane Assembly: A Linkage Targeted by Many Hereditary Hemolytic Anemias? Experimental And Molecular Pathology 2001, 70: 215-230. PMID: 11418000, DOI: 10.1006/exmp.2001.2377.Peer-Reviewed Original Research
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
1992
Cytostellin: a novel, highly conserved protein that undergoes continuous redistribution during the cell cycle
Warren S, Landolfi A, Curtis C, Morrow J. Cytostellin: a novel, highly conserved protein that undergoes continuous redistribution during the cell cycle. Journal Of Cell Science 1992, 103: 381-388. PMID: 1478941, DOI: 10.1242/jcs.103.2.381.Peer-Reviewed Original ResearchConceptsMitotic spindle apparatusSpindle apparatusLower eukaryotic cellsOnset of prophaseEukaryotic cellsDaughter cellsCytoplasmic proteinsMammalian cellsMonoclonal antibody H5Interphase nucleiTelophase cellsNuclease digestionCell cycleImmunofluorescence microscopyImmunoblot analysisCell processesProteinNascent nucleiSalt extractionImmunoaffinity chromatographyCellsDistinct subsetsNucleusAnaphaseProphaseKaryoplasmic 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