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 spectrinDynactin-Dependent, Dynein-Driven Vesicle Transport in the Absence of Membrane Proteins A Role for Spectrin and Acidic Phospholipids
Muresan V, Stankewich M, Steffen W, Morrow J, Holzbaur E, Schnapp B. Dynactin-Dependent, Dynein-Driven Vesicle Transport in the Absence of Membrane Proteins A Role for Spectrin and Acidic Phospholipids. Molecular Cell 2001, 7: 173-183. PMID: 11172722, DOI: 10.1016/s1097-2765(01)00165-4.Peer-Reviewed Original ResearchConceptsVesicle transportAcidic phospholipidsAxonal vesiclesProtein-free liposomesAbsence of membranesPH domainDependent motilityCytosolic factorsDynactinSpectrinEssential roleSpectrin polypeptidesVesiclesMembranePhospholipidsAxonal transportMotilitySoluble componentsContext of liposomesDyneinCytosolPolypeptideTransportRoleRetrograde axonal transport