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
1998
ADP ribosylation factor regulates spectrin binding to the Golgi complex
Godi A, Santone I, Pertile P, Devarajan P, Stabach P, Morrow J, Di Tullio G, Polishchuk R, Petrucci T, Luini A, De Matteis M. ADP ribosylation factor regulates spectrin binding to the Golgi complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 8607-8612. PMID: 9671725, PMCID: PMC21123, DOI: 10.1073/pnas.95.15.8607.Peer-Reviewed Original ResearchConceptsADP-ribosylation factorGolgi complexRibosylation factorG proteinsVesicular stomatitis virus G proteinPleckstrin homology domainSmall G proteinsPH domain interactionBinding of spectrinVirus G proteinGolgi spectrinHomology domainPH domainCoat proteinDocking siteDomain interactionsGolgiEndoplasmic reticulumPtdInsP2 levelsDomain IPhospholipase DSpectrinGolgi fractionsProteinPtdInsP2
1997
Na,K-ATPase transport from endoplasmic reticulum to Golgi requires the Golgi spectrin–ankyrin G119 skeleton in Madin Darby canine kidney cells
Devarajan P, Stabach P, De Matteis M, Morrow J. Na,K-ATPase transport from endoplasmic reticulum to Golgi requires the Golgi spectrin–ankyrin G119 skeleton in Madin Darby canine kidney cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 10711-10716. PMID: 9380700, PMCID: PMC23456, DOI: 10.1073/pnas.94.20.10711.Peer-Reviewed Original ResearchConceptsMembrane proteinsEndoplasmic reticulumSpectrin skeletonVesicular tubular clustersActin-binding domainSpecific membrane proteinsMadin-Darby canine kidney cellsK-ATPase transportCanine kidney cellsDynactin complexVesicle traffickingCargo proteinsGolgi spectrinTrafficking systemBeta-COPMembrane compartmentsTransport of alphaAdapter proteinCis-GolgiGolgi membranesGolgi stacksDocking complexBetaI spectrinGolgiBeta NA