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 spectrin
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
1994
A 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