1996
Characterization of a Nuclear Protein Conferring Brefeldin A Resistance in Schizosaccharomyces pombe (∗)
Turi T, Mueller U, Sazer S, Rose J. Characterization of a Nuclear Protein Conferring Brefeldin A Resistance in Schizosaccharomyces pombe (∗). Journal Of Biological Chemistry 1996, 271: 9166-9171. PMID: 8621569, DOI: 10.1074/jbc.271.15.9166.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntifungal AgentsBase SequenceBrefeldin ACell CompartmentationConsensus SequenceCyclopentanesDNA PrimersDrug Resistance, MicrobialFungal ProteinsGenes, FungalGolgi ApparatusGTP-Binding ProteinsMolecular Sequence DataNuclear ProteinsPhosphoproteinsRan GTP-Binding ProteinRestriction MappingSchizosaccharomycesSequence AlignmentSequence Homology, Amino AcidConceptsNuclear pore complexWild type SchizosaccharomycesPore complexS. pombeSchizosaccharomyces pombeProtein RanBP1Essential proteinsGolgi complexEndoplasmic reticulumProtein secretionPeptide motifsMultiple copiesNovel mechanismGenesProteinPombeA ResistanceBrefeldinDrug resistanceSchizosaccharomycesYrb1RanBP1HomologyComplexesReticulum
1994
Brefeldin A sensitivity and resistance in Schizosaccharomyces pombe. Isolation of multiple genes conferring resistance.
Turi T, Webster P, Rose J. Brefeldin A sensitivity and resistance in Schizosaccharomyces pombe. Isolation of multiple genes conferring resistance. Journal Of Biological Chemistry 1994, 269: 24229-24236. PMID: 7929079, DOI: 10.1016/s0021-9258(19)51072-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntifungal AgentsBrefeldin ACyclopentanesDrug Resistance, MicrobialFungal ProteinsGolgi ApparatusKaryopherinsMolecular Sequence DataMutationPancreatitis-Associated ProteinsPhenotypePlasmidsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSchizosaccharomycesSequence Homology, Amino AcidConceptsBFA resistanceEffects of BFABrefeldin AGolgi complexMammalian cellsTranscription factor Pap1Fission yeast SchizosaccharomycesFungal metabolite brefeldin ASeparate linkage groupsWild-type cellsChromatin structureYeast SchizosaccharomycesSchizosaccharomyces pombeAP1 proteinLinkage groupsGolgi morphologyAnimal cellsMultiple genesDifferent genesGenetic analysisEndoplasmic reticulumProtein secretionGenesType cellsMutants
1993
Dynamic equilibrium between vesicular stomatitis virus glycoprotein monomers and trimers in the Golgi and at the cell surface
Zagouras P, Rose J. Dynamic equilibrium between vesicular stomatitis virus glycoprotein monomers and trimers in the Golgi and at the cell surface. Journal Of Virology 1993, 67: 7533-7538. PMID: 8230472, PMCID: PMC238219, DOI: 10.1128/jvi.67.12.7533-7538.1993.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, ViralAntibody SpecificityBiological TransportBrefeldin ACell CompartmentationCell MembraneCells, CulturedCricetinaeCyclopentanesGolgi ApparatusHexosaminidasesMembrane GlycoproteinsMutationPostural BalanceProtein ConformationProtein Processing, Post-TranslationalVesicular stomatitis Indiana virusViral Envelope ProteinsConceptsEndoplasmic reticulumHeterotrimer formationG proteinsMutant G proteinsG protein trimersVesicular stomatitis virus glycoproteinG protein subunitsVSV G proteinProtein moleculesG protein moleculesWild-type trimersMutant proteinsCytoplasmic domainCellular compartmentsCoexpression experimentsGlycoprotein monomersLonger chase periodsPlasma membraneProtein subunitsMu proteinProtein trimerForms trimersCell surfaceMonomeric subunitsProtein
1992
Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
Brown D, Rose J. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 1992, 68: 533-544. PMID: 1531449, DOI: 10.1016/0092-8674(92)90189-j.Peer-Reviewed Original ResearchConceptsBasolateral marker proteinsCertain membrane proteinsApical cell surfaceDetergent-insoluble formGlycosylphosphatidyl inositol (GPI) anchorMembrane subdomainsMembrane proteinsIntracellular associationGolgi complexMicrodomains formGolgi apparatusInositol anchorMarker proteinsCell surfaceProteinApical surfaceEpithelial cellsGPIGlycosphingolipidsComplexesVesiclesLysatesGlycolipidsSortingMembrane
1989
Carboxy-terminal SEKDEL sequences retard but do not retain two secretory proteins in the endoplasmic reticulum.
Zagouras P, Rose J. Carboxy-terminal SEKDEL sequences retard but do not retain two secretory proteins in the endoplasmic reticulum. Journal Of Cell Biology 1989, 109: 2633-2640. PMID: 2592401, PMCID: PMC2115906, DOI: 10.1083/jcb.109.6.2633.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumSEKDEL sequenceSecretory proteinsSequence Ser-GluAmino acidsMonkey COS cellsOligonucleotide-directed mutagenesisLast amino acidFirst amino acidProtein exitIndirect immunofluorescence microscopyAnimal cellsCOS cellsCOOH terminusAlpha subunitProtein structureGolgi apparatusLys-AspImmunofluorescence microscopyOligosaccharide processingProteinReticulumSEKDELSer-GluSpecific interactions
1985
Glycosylation allows cell-surface transport of an anchored secretory protein
Guan J, Machamer C, Rose J. Glycosylation allows cell-surface transport of an anchored secretory protein. Cell 1985, 42: 489-496. PMID: 3928168, DOI: 10.1016/0092-8674(85)90106-0.Peer-Reviewed Original ResearchConceptsCell surfaceProtein transportMutant proteinsCarboxy-terminal extensionCell surface transportVesicular stomatitis virus glycoproteinMembrane-anchored formSingle amino acidCytoplasmic domainHybrid geneGlycosylation sitesConsensus sequenceSecretory proteinsGolgi apparatusCellular membranesAmino acidsProteinRandom sitesGlycosylationVirus glycoproteinRat growth hormoneGrowth hormoneTransmembraneGenesSitesStructural requirements of a membrane-spanning domain for protein anchoring and cell surface transport
Adams G, Rose J. Structural requirements of a membrane-spanning domain for protein anchoring and cell surface transport. Cell 1985, 41: 1007-1015. PMID: 3924407, DOI: 10.1016/s0092-8674(85)80081-7.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological TransportCell LineCell MembraneEndoplasmic ReticulumFluorescent Antibody TechniqueGlycoside HydrolasesGolgi ApparatusMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMembrane GlycoproteinsMembrane ProteinsMutationPalmitic AcidPalmitic AcidsPlasmidsViral Envelope ProteinsViral ProteinsConceptsMembrane-spanning domainsCell surface transportTransmembrane domainG proteinsAmino acidsVesicular stomatitis virus glycoproteinOligonucleotide-directed mutagenesisHydrophobic amino acidsMembrane anchoringProtein anchoringIntracellular membranesTransmembrane configurationEndoplasmic reticulumCell surfaceProteinVirus glycoproteinDNASurface transportStructural requirementsDomainMutagenesisAcidReticulumAnchoringTransport
1984
Conversion of a secretory protein into a transmembrane protein results in its transport to the golgi complex but not to the cell surface
Guan J, Rose J. Conversion of a secretory protein into a transmembrane protein results in its transport to the golgi complex but not to the cell surface. Cell 1984, 37: 779-787. PMID: 6589049, DOI: 10.1016/0092-8674(84)90413-6.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsMembrane proteinsSecretory proteinsFusion proteinCell surfaceVesicular stomatitis virus glycoproteinRat growth hormoneMembrane spanningCytoplasmic domainCDNA clonesCarboxy terminusHybrid geneEucaryotic cellsTransmembrane configurationGolgi apparatusProtein resultsProteinMicrosomal membranesVirus glycoproteinRapid secretionMembranePalmitic acidGolgiGenesTerminus