2001
[42] ADP-ribosylation factor (ARF) as regulator of spectrin assembly at Golgi complex
De Matteis M, Morrow J. [42] ADP-ribosylation factor (ARF) as regulator of spectrin assembly at Golgi complex. Methods In Enzymology 2001, 329: 405-416. PMID: 11210560, DOI: 10.1016/s0076-6879(01)29101-0.Peer-Reviewed Original ResearchMeSH KeywordsADP-Ribosylation FactorsAnimalsCell LineCell Membrane PermeabilityCoat Protein Complex IDNA PrimersElectrophoresis, Polyacrylamide GelEscherichia coliFluorescent Antibody TechniqueGenetic VectorsGolgi ApparatusIntracellular MembranesPeptide FragmentsProtein BindingRecombinant Fusion ProteinsSpectrinConceptsADP-ribosylation factorGolgi membranesSpectrin peptidesPermeabilized cultured cellsBinding of spectrinCultured cell linesDifferent functional domainsSpectrin assemblySequence motifsRibosylation factorIndirect immunofluorescent microscopyFunctional domainsIntracellular distributionCultured cellsSpectrinΒIII spectrinImmunofluorescence analysisCell linesGolgiImmunofluorescent microscopyExperimental strategiesPeptidesMembraneCellsOrganelles
2000
Spectrin tethers and mesh in the biosynthetic pathway.
De Matteis M, Morrow J. Spectrin tethers and mesh in the biosynthetic pathway. Journal Of Cell Science 2000, 113 ( Pt 13): 2331-43. PMID: 10852813, DOI: 10.1242/jcs.113.13.2331.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCytoskeletonGolgi ApparatusHumansIntracellular MembranesProtein BiosynthesisSpectrinConceptsSecretory pathwayMembrane proteinsSmall GTPase ArfEarly secretory pathwayDynamics of organellesGolgi dynamicsProtein traffickingOrganelle functionGolgi structurePhosphoinositide levelsGolgi membranesBiosynthetic pathwayMacromolecular complexesCytosolic proteinsAdapter moleculeSpectrin skeletonIntracellular transportOrganellesSpectrinDirect interactionProteinKey playersRecent discoveryGolgiSimilar role
1998
A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles
Stankewich M, Tse W, Peters L, Ch’ng Y, John K, Stabach P, Devarajan P, Morrow J, Lux S. A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 14158-14163. PMID: 9826670, PMCID: PMC24343, DOI: 10.1073/pnas.95.24.14158.Peer-Reviewed Original ResearchConceptsBetaIII spectrinGene mapsMembrane skeletonEndoplasmic reticulum marker calnexinPlasma membrane skeletonPleckstrin homology domainTrans-Golgi networkHuman brain cDNASyntenic regionsGene familyProtein 4.1Membrane associationCompartment markersImportant structural componentDa proteinSelf-association siteGolgi membranesHomology searchCDNA endsRapid amplificationUnidentified isoformChromosome 19Liver Golgi membranesGenBank databaseVesicle markersThe role of ankyrin and spectrin in membrane transport and domain formation
De Matteis M, Morrow J. The role of ankyrin and spectrin in membrane transport and domain formation. Current Opinion In Cell Biology 1998, 10: 542-549. PMID: 9719877, DOI: 10.1016/s0955-0674(98)80071-9.Peer-Reviewed Original ResearchConceptsAnterograde protein traffickingRole of ankyrinADP-ribosylation factorGolgi integrityProtein traffickingSpecific functional domainsSpectrin functionSecretory pathwayMotor proteinsFunctional domainsGolgi complexMembrane transportNovel insightsSpectrinRecent discoveryDomain formationAnkyrinTraffickingProteinPathwayFunctionComplexesDiscoveryDomainIdentificationADP 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