1998
The 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 ResearchMeSH KeywordsADP-Ribosylation FactorsAnkyrinsBiological TransportCell CompartmentationCell MembraneGolgi ApparatusGTP-Binding ProteinsPhosphatidylinositolsSpectrinConceptsAnterograde 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