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 subunitsProteinCell fusion by the envelope glycoproteins of persistent measles viruses which caused lethal human brain disease
Cattaneo R, Rose J. Cell fusion by the envelope glycoproteins of persistent measles viruses which caused lethal human brain disease. Journal Of Virology 1993, 67: 1493-1502. PMID: 8437226, PMCID: PMC237519, DOI: 10.1128/jvi.67.3.1493-1502.1993.Peer-Reviewed Original ResearchMeSH KeywordsAutopsyBacteriophage T7Biological TransportBrain DiseasesCell FusionCell LineCloning, MolecularDNA, ViralGlycosylationHeLa CellsHemagglutinins, ViralHumansMeaslesMeasles virusOligosaccharidesPromoter Regions, GeneticProtein ConformationProtein Processing, Post-TranslationalRecombinant ProteinsRNA, ViralViral Envelope ProteinsViral Fusion ProteinsViral InterferenceViral Matrix ProteinsVirulenceConceptsIntegral membrane proteinsH proteinCell fusionMembrane proteinsIntracellular domainViral buddingM proteinHS-protein interactionsF protein functionProtein interactionsMV genesIntracellular transportFusion proteinOligosaccharide modificationViral envelope proteinsMatrix proteinsHuman brain diseasesProteinMeasles virusReduced expressionEnvelope proteinPersistent measles virusBuddingSyncytium formationDisease development
1992
Human immunodeficiency virus type 1 glycoprotein precursor retains a CD4-p56lck complex in the endoplasmic reticulum
Crise B, Rose J. Human immunodeficiency virus type 1 glycoprotein precursor retains a CD4-p56lck complex in the endoplasmic reticulum. Journal Of Virology 1992, 66: 2296-2301. PMID: 1548763, PMCID: PMC289024, DOI: 10.1128/jvi.66.4.2296-2301.1992.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumHuman immunodeficiency virusTyrosine kinaseHIV infectionCD4-p56lck complexTransient expression systemGlycoprotein precursorCytoplasmic tyrosine kinaseConfocal immunofluorescence microscopyExpression of CD4HIV-1 gp160Cell surface glycoproteinExpression of gp160Cytoplasmic facePlasma membraneT cell activationExpression systemHeLa cellsImmunofluorescence microscopyCell surfaceImmunodeficiency virusT lymphocytesT cellsLymphocyte killingCD4
1991
Dissociation and reassociation of oligomeric viral glycoprotein subunits in the endoplasmic reticulum
Zagouras P, Ruusala A, Rose J. Dissociation and reassociation of oligomeric viral glycoprotein subunits in the endoplasmic reticulum. Journal Of Virology 1991, 65: 1976-1984. PMID: 1848313, PMCID: PMC240033, DOI: 10.1128/jvi.65.4.1976-1984.1991.Peer-Reviewed Original ResearchConceptsWild-type ratesEndoplasmic reticulumMutant subunitsG proteinsCell surfaceG protein trimersWild-type subunitsFormation of heterotrimersWild-type moleculeWild-type trimersMutant proteinsRetention signalProtein trimerHeterotrimerSubunitsGlycoprotein subunitsProteinReticulumGlycoprotein formTrimerTransport blockHomotrimersReassociation
1990
Prevention of HIV-1 glycoprotein transport by soluble CD4 retained in the endoplasmic reticulum
Buonocore L, Rose J. Prevention of HIV-1 glycoprotein transport by soluble CD4 retained in the endoplasmic reticulum. Nature 1990, 345: 625-628. PMID: 2190096, DOI: 10.1038/345625a0.Peer-Reviewed Original ResearchConceptsCD4 moleculeHIV glycoproteinSoluble CD4 moleculesHuman immunodeficiency virusCellular CD4 receptorWild-type CD4Human T cellsInfectious HIVCD4 cellsImmunodeficiency virusSoluble CD4T cellsTherapeutic strategiesCD4 receptorImmunization procedureEnvelope glycoproteinVirus entrySurface expressionCD4HIVIdeal targetEndoplasmic reticulumVirusExpressionCells
1989
Mechanism of Membrane Anchoring Affects Polarized Expression of Two Proteins in MDCK Cells
Brown D, Crise B, Rose J. Mechanism of Membrane Anchoring Affects Polarized Expression of Two Proteins in MDCK Cells. Science 1989, 245: 1499-1501. PMID: 2571189, DOI: 10.1126/science.2571189.Peer-Reviewed Original ResearchConceptsMembrane anchorageGPI anchorBasolateral plasma membrane domainsSorting of proteinsPlasma membrane domainsPolarized epithelial cellsClass of proteinsBasolateral surfaceVesicular stomatitis virus glycoproteinMembrane anchoringCytoplasmic domainMembrane domainsMembrane proteinsPolypeptide sequenceTransport signalVSV GPolarized expressionMDCK cellsApical expressionProteinApical surfaceEpithelial cellsVirus glycoproteinPlacental alkaline phosphataseExpressionA single-amino-acid substitution eliminates the stringent carbohydrate requirement for intracellular transport of a viral glycoprotein
Pitta A, Rose J, Machamer C. A single-amino-acid substitution eliminates the stringent carbohydrate requirement for intracellular transport of a viral glycoprotein. Journal Of Virology 1989, 63: 3801-3809. PMID: 2760984, PMCID: PMC250973, DOI: 10.1128/jvi.63.9.3801-3809.1989.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsBiological TransportCell MembraneGlycosylationMembrane GlycoproteinsMutationProtein ConformationTunicamycinViral Envelope Proteins
1988
Regulation of Protein Export From the Endoplasmic Reticulum
Rose J, Doms R. Regulation of Protein Export From the Endoplasmic Reticulum. Annual Review Of Cell And Developmental Biology 1988, 4: 257-288. PMID: 3058161, DOI: 10.1146/annurev.cb.04.110188.001353.Peer-Reviewed Original ResearchDifferential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein.
Doms R, Ruusala A, Machamer C, Helenius J, Helenius A, Rose J. Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein. Journal Of Cell Biology 1988, 107: 89-99. PMID: 2839523, PMCID: PMC2115181, DOI: 10.1083/jcb.107.1.89.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalAntibody SpecificityBiological TransportCell LineCentrifugation, Density GradientElectrophoresis, Polyacrylamide GelEndoplasmic ReticulumGlycosylationImmunoassayKineticsMacromolecular SubstancesMembrane GlycoproteinsMutationProtein ConformationTransfectionVesicular stomatitis Indiana virusViral Envelope ProteinsViral Matrix ProteinsConceptsG proteinsMutant proteinsCytoplasmic domainMutant G proteinsVesicular stomatitis virus G proteinIntegral membrane proteinsWild-type proteinTrimer formationVesicular stomatitis virus glycoproteinVirus G proteinAltered glycosylation patternConformation-specific antibodiesTail mutationsMembrane proteinsMin of synthesisOligomeric assembliesQuaternary structureMature formEndoplasmic reticulumInitial foldingGlycosylation patternsCell surfaceEctodomainProteinFoldingInfluence of new glycosylation sites on expression of the vesicular stomatitis virus G protein at the plasma membrane.
Machamer C, Rose J. Influence of new glycosylation sites on expression of the vesicular stomatitis virus G protein at the plasma membrane. Journal Of Biological Chemistry 1988, 263: 5948-5954. PMID: 2833523, DOI: 10.1016/s0021-9258(18)60658-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBinding SitesBiological TransportCell LineCell MembraneCloning, MolecularDNA, RecombinantFluorescent Antibody TechniqueGlycosylationImmunosorbent TechniquesIodine RadioisotopesLactoperoxidaseMembrane GlycoproteinsMolecular Sequence DataMutationOligosaccharidesTransfectionTunicamycinVesicular stomatitis Indiana virusViral Envelope ProteinsViral Matrix ProteinsConceptsVesicular stomatitis virus G proteinVirus G proteinG proteinsConsensus sitesIntracellular transportWild-type G proteinWild-type proteinOligonucleotide-directed mutagenesisNew consensus sitePlasma membrane glycoproteinsMutant proteinsNew glycosylation siteNew sitesAsparagine-linked oligosaccharidesPlasma membraneGlycosylation sitesMembrane glycoproteinsInhibition of transportProteinPolypeptide backboneNormal sitesIndirect roleOligosaccharidesExpressionSitesVesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding.
Machamer C, Rose J. Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding. Journal Of Biological Chemistry 1988, 263: 5955-5960. PMID: 2833524, DOI: 10.1016/s0021-9258(18)60659-3.Peer-Reviewed Original ResearchBinding SitesBiological TransportCell LineCell MembraneDisulfidesDNA, RecombinantEndoplasmic ReticulumFluorescent Antibody TechniqueGlycosylationHexosaminidasesImmunosorbent TechniquesIodine RadioisotopesLactoperoxidaseMembrane GlycoproteinsMutationOligosaccharidesProtein ConformationStructure-Activity RelationshipTemperatureTransfectionVesicular stomatitis Indiana virusViral Envelope ProteinsViral Matrix Proteins
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 requirementsDomainMutagenesisAcidReticulumAnchoringTransportIncorporation of a charged amino acid into the membrane-spanning domain blocks cell surface transport but not membrane anchoring of a viral glycoprotein.
Adams G, Rose J. Incorporation of a charged amino acid into the membrane-spanning domain blocks cell surface transport but not membrane anchoring of a viral glycoprotein. Molecular And Cellular Biology 1985, 5: 1442-1448. PMID: 2993864, PMCID: PMC366875, DOI: 10.1128/mcb.5.6.1442.Peer-Reviewed Original ResearchConceptsMembrane anchoringG proteinsAmino acidsCell surfaceIsoleucine residueMembrane-spanning domainsCell surface transportVesicular stomatitis virus glycoproteinOligonucleotide-directed mutagenesisAmino acid sequenceUncharged amino acidsDetectable protein levelsHydrophobic amino acidsAnimal cellsCDNA clonesIntracellular membranesAcid sequencePunctate patternGolgi regionProteinContinuous stretchVesicular patternProtein levelsViral glycoproteinsVirus glycoproteinA single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein
Gallione C, Rose J. A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein. Journal Of Virology 1985, 54: 374-382. PMID: 2985803, PMCID: PMC254807, DOI: 10.1128/jvi.54.2.374-382.1985.Peer-Reviewed Original ResearchConceptsCDNA clonesHydrophobic domainAmino acidsCell surface transportSingle amino acid substitutionVesicular stomatitis virus glycoproteinWild-type parent strainDNA sequence analysisPolar amino acidsHydrophobic amino acidsAmino acid changesAmino acid substitutionsProtein transportDNA sequencesNonpermissive temperatureVesicular stomatitis virusCOS cellsNonconservative substitutionsSequence analysisSpontaneous revertantsAcid substitutionsAcid changesSingle substitutionTransport defectStomatitis virus
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