2001
Vesicular Stomatitis Virus Glycoprotein Containing the Entire Green Fluorescent Protein on Its Cytoplasmic Domain Is Incorporated Efficiently into Virus Particles
Dalton K, Rose J. Vesicular Stomatitis Virus Glycoprotein Containing the Entire Green Fluorescent Protein on Its Cytoplasmic Domain Is Incorporated Efficiently into Virus Particles. Virology 2001, 279: 414-421. PMID: 11162797, DOI: 10.1006/viro.2000.0736.Peer-Reviewed Original ResearchConceptsLarge cytoplasmic domainCytoplasmic domainVSV G proteinVesicular stomatitis virusGreen fluorescent proteinG proteinsGFP proteinWild-type G proteinFluorescent proteinShort cytoplasmic domainVesicular stomatitis virus glycoproteinStrong selectionVirus particlesExtra genesHeterotrimeric proteinGFP geneProtein sequencesWild-type virusFluorescent virus particlesStop codonVirus assemblyInfectious cloneGenesViral membraneAmino acids
1998
Requirement for a non‐specific glycoprotein cytoplasmic domain sequence to drive efficient budding of vesicular stomatitis virus
Schnell M, Buonocore L, Boritz E, Ghosh H, Chernish R, Rose J. Requirement for a non‐specific glycoprotein cytoplasmic domain sequence to drive efficient budding of vesicular stomatitis virus. The EMBO Journal 1998, 17: 1289-1296. PMID: 9482726, PMCID: PMC1170477, DOI: 10.1093/emboj/17.5.1289.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCD4 AntigensCell LineCell MembraneCricetinaeCytopathogenic Effect, ViralCytoplasmHumansMembrane GlycoproteinsMolecular Sequence DataMutationRecombinant Fusion ProteinsSequence DeletionSerial PassageVesicular stomatitis Indiana virusViral Envelope ProteinsViral ProteinsVirionConceptsCytoplasmic domainEfficient buddingAmino acidsCytoplasmic domain deletion mutantEfficient virus buddingShort cytoplasmic domainCytoplasmic domain sequencesDomain deletion mutantVesicular stomatitis virus glycoproteinChimeric G proteinsTransmembrane domainDeletion mutantsInternal viral componentsVirus buddingGlycoprotein arrayVesicular stomatitis virusDomain sequencesViral buddingVirion morphologyG proteinsMatrix proteinsVSV GHuman CD4 proteinForeign sequencesBudding
1994
Stimulation of Heterologous Protein Degradation by the Vpu Protein of HIV-1 Requires the Transmembrane and Cytoplasmic Domains of CD4
Buonocore L, Turi T, Crise B, Rose J. Stimulation of Heterologous Protein Degradation by the Vpu Protein of HIV-1 Requires the Transmembrane and Cytoplasmic Domains of CD4. Virology 1994, 204: 482-486. PMID: 8091684, DOI: 10.1006/viro.1994.1560.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCD4 AntigensGlycoproteinsHeLa CellsHIV-1Human Immunodeficiency Virus ProteinsHumansMembrane GlycoproteinsMolecular Sequence DataProtein Structure, TertiaryRecombinant Fusion ProteinsRecombinant ProteinsViral Envelope ProteinsViral Regulatory and Accessory ProteinsConceptsCytoplasmic domainTransmembrane domainHybrid proteinHeterologous protein degradationVesicular stomatitis virus glycoproteinRapid degradationAdditional hybridsProtein degradationExtracellular domainProtein VpuRelated sequencesVpu proteinDegradation systemEndoplasmic reticulumVSV GVpu expressionProteinVpuTransmembraneVirus glycoproteinRecent studiesDomainHuman immunodeficiency virus type 1Immunodeficiency virus type 1DegradationMutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotein that affect fusion activity
Owens R, Burke C, Rose J. Mutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotein that affect fusion activity. Journal Of Virology 1994, 68: 570-574. PMID: 8254774, PMCID: PMC236324, DOI: 10.1128/jvi.68.1.570-574.1994.Peer-Reviewed Original ResearchConceptsTransmembrane domainFusion activityVesicular stomatitis virus G proteinMembrane-spanning domainsCell surfaceSpecific amino acid sequencesAmino acid sequenceMembrane fusion activityAmino acid residuesMembrane fusion processCytoplasmic tail domainVirus G proteinCytoplasmic domainMutagenic analysisAcid sequenceChimeric proteinBasic residuesProtein ectodomainAcid residuesG proteinsHeLa cellsVirus envelope glycoproteinLipid bilayersProteinGp41 transmembrane
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 subunitsProteinCytoplasmic domain requirement for incorporation of a foreign envelope protein into vesicular stomatitis virus
Owens R, Rose J. Cytoplasmic domain requirement for incorporation of a foreign envelope protein into vesicular stomatitis virus. Journal Of Virology 1993, 67: 360-365. PMID: 8093220, PMCID: PMC237371, DOI: 10.1128/jvi.67.1.360-365.1993.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCD4-Positive T-LymphocytesCell FusionFluorescent Antibody TechniqueGene Products, envHIV Envelope Protein gp120HIV Envelope Protein gp41HIV-1Membrane GlycoproteinsMolecular Sequence DataRecombinant Fusion ProteinsStructure-Activity RelationshipVesicular stomatitis Indiana virusViral Envelope ProteinsViral Fusion ProteinsConceptsHIV-1 envelope proteinEnvelope proteinAnti-HIV-1 seraHuman immunodeficiency virus type 1 (HIV-1) envelope proteinG proteinsHIV-1 entryVesicular stomatitis virus particlesHIV-1Vesicular stomatitis virusEnvelope glycoproteinWild-type G proteinStomatitis virusVSV particlesVSV G proteinVirus particlesTemperature-sensitive mutantPseudotypesSimultaneous expressionTransmembrane domainCytoplasmic domainCytoplasmic tailDefective transportVSV
1992
Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor.
Crise B, Rose J. Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor. Journal Of Biological Chemistry 1992, 267: 13593-13597. PMID: 1618861, DOI: 10.1016/s0021-9258(18)42253-3.Peer-Reviewed Original ResearchConceptsCytoplasmic domainBinding of p56lckHuman immunodeficiency virus receptorCell surface glycoprotein CD4Palmitoylation sitesCysteine residuesThioester linkageGlycoprotein CD4HeLa cellsCell surfaceVirus receptorProteinFatty acidsMutationsCysteineExpression of CD4Cys397Palmitic acidCys394P56lckTransmembraneCD4AcidPalmitateDomain
1991
Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein
Whitt M, Buonocor L, Prehaud C, Rose J. Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein. Virology 1991, 185: 681-688. PMID: 1660200, DOI: 10.1016/0042-6822(91)90539-n.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, ViralBase SequenceCell LineCentrifugation, Density GradientCricetinaeFlow CytometryGenetic Complementation TestGlycoproteinsHumansHydrogen-Ion ConcentrationKineticsMacromolecular SubstancesMembrane FusionMembrane GlycoproteinsMiceMolecular Sequence DataPlasmidsRabies virusRecombinant Fusion ProteinsVesicular stomatitis Indiana virusViral Envelope ProteinsViral Fusion ProteinsConceptsVSV G proteinG protein trimersMembrane fusion activityVirus G proteinG proteinsRabies G proteinFusion activityHybrid proteinProtein trimerVesicular stomatitis virus G proteinVirus glycoproteinRabies virus glycoproteinCytoplasmic domainMembrane fusionExtracellular domainHeLa cellsRabies virus G proteinCell surfaceProteinVSV particlesSucrose gradientsVSV infectivityGlycoproteinSpike glycoproteinChemical crosslinkingFatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions
Whitt M, Rose J. Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions. Virology 1991, 185: 875-878. PMID: 1660205, DOI: 10.1016/0042-6822(91)90563-q.Peer-Reviewed Original ResearchConceptsFatty acid acylationVSV G proteinMembrane fusion activityVesicular stomatitis virusG proteinsWild-type G proteinFusion activityWild-type proteinTemperature-sensitive mutantCytoplasmic domainTransient expressionPresence of palmitateVSV virionsIndiana serotypeHeLa cellsExpression of CSProteinStomatitis virusLife cycleSyncytium formationExpressionMutantsAcylationVirionsVirus
1990
Short related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56lck tyrosine protein kinase.
Shaw A, Chalupny J, Whitney J, Hammond C, Amrein K, Kavathas P, Sefton B, Rose J. Short related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56lck tyrosine protein kinase. Molecular And Cellular Biology 1990, 10: 1853-1862. PMID: 2109184, PMCID: PMC360530, DOI: 10.1128/mcb.10.5.1853.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigens, Differentiation, T-LymphocyteBase SequenceCD4 AntigensCD8 AntigensCysteineCytoplasmDNA Mutational AnalysisHumansIn Vitro TechniquesLymphocyte Specific Protein Tyrosine Kinase p56(lck)Molecular Sequence DataProtein BindingProtein-Tyrosine KinasesSignal TransductionStructure-Activity RelationshipConceptsAmino-terminal domainTyrosine protein kinaseCytoplasmic domainProtein kinaseBinding of p56lckCommon sequence motifsRelated amino acid sequencesAmino acid sequenceDisulfide bond formationCD8 alphaAmino acid residuesSequence motifsHybrid proteinCysteine residuesAcid sequenceUnrelated proteinsAlpha proteinRelated sequencesAcid residuesCD4 sequencesP56lckGlycoprotein CD4HeLa cellsProteinKinaseShort Related Sequences in the Cytoplasmic Domains of CD4 and CD8 Mediate Binding to the Amino-Terminal Domain of the p56 lck Tyrosine Protein Kinase
Shaw A, Chalupny J, Whitney J, Hammond C, Amrein K, Kavathas P, Sefton B, Rose J. Short Related Sequences in the Cytoplasmic Domains of CD4 and CD8 Mediate Binding to the Amino-Terminal Domain of the p56 lck Tyrosine Protein Kinase. Molecular And Cellular Biology 1990, 10: 1853-1862. DOI: 10.1128/mcb.10.5.1853-1862.1990.Peer-Reviewed Original ResearchAmino-terminal domainTyrosine protein kinaseCytoplasmic domainP56 lckProtein kinaseCommon sequence motifsRelated amino acid sequencesAmino acid sequenceDisulfide bond formationAmino acid residuesSequence motifsHybrid proteinCysteine residuesAcid sequenceUnrelated proteinsRelated sequencesAcid residuesCD4 sequencesLckGlycoprotein CD4HeLa cellsMediate bindingProteinKinaseSequence
1989
Oligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein
Crise B, Ruusala A, Zagouras P, Shaw A, Rose J. Oligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein. Journal Of Virology 1989, 63: 5328-5333. PMID: 2555557, PMCID: PMC251199, DOI: 10.1128/jvi.63.12.5328-5333.1989.Peer-Reviewed Original ResearchMeSH KeywordsAcetylglucosaminidaseAmino Acid SequenceBase SequenceCentrifugation, Density GradientCodonElectrophoresis, Polyacrylamide GelGlycolipidsHeLa CellsHumansKineticsMacromolecular SubstancesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMembrane GlycoproteinsMolecular Sequence DataRestriction MappingSolubilityVesicular stomatitis Indiana virusViral Envelope ProteinsConceptsG proteinsWild-type G proteinAmino acidsC-terminal amino acidsVesicular stomatitis virus glycoproteinMutant proteinsCytoplasmic domainAnchor sequenceExtracellular domainGolgi apparatusEndoplasmic reticulumCell surfaceTrimer formationProteinPhospholipase C.TransmembraneVirus glycoproteinSoluble formStructural informationSequenceGlycoproteinNormal transmembraneRate of transportGlycoprotein formThy-1.1The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain
Shaw A, Amrein K, Hammond C, Stern D, Sefton B, Rose J. The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain. Cell 1989, 59: 627-636. PMID: 2582490, DOI: 10.1016/0092-8674(89)90008-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCD4 AntigensCytoplasmHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Macromolecular SubstancesMembrane GlycoproteinsMolecular Sequence DataMutationOligonucleotide ProbesPhosphoproteinsPlasmidsProtein BindingProtein MultimerizationProtein-Tyrosine KinasesT-LymphocytesTransfectionConceptsAmino-terminal domainCytoplasmic domainTyrosine protein kinase p56lckUnique amino-terminal domainT cell-specific proteinsTyrosine protein kinaseSpecific transmembrane proteinsCell-specific proteinsIntracellular tyrosine kinaseAmino-terminal residuesCarboxy-terminal residuesTransmembrane proteinCytoplasmic tailSrc familyProtein kinaseKinase p56lckTyrosine kinaseHeLa cellsCell surfaceProteinDeleted formsSurface glycoproteinP56lckKinaseResiduesMechanism 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 phosphataseExpressionGlycoprotein cytoplasmic domain sequences required for rescue of a vesicular stomatitis virus glycoprotein mutant
Whitt M, Chong L, Rose J. Glycoprotein cytoplasmic domain sequences required for rescue of a vesicular stomatitis virus glycoprotein mutant. Journal Of Virology 1989, 63: 3569-3578. PMID: 2547986, PMCID: PMC250946, DOI: 10.1128/jvi.63.9.3569-3578.1989.Peer-Reviewed Original ResearchConceptsCytoplasmic domainG proteinsAmino acidsWild-type G proteinNormal cytoplasmic domainG protein mutantsCytoplasmic domain sequencesVesicular stomatitis virus glycoproteinVSV G proteinTemperature-sensitive mutantViral G proteinSurface expressionG protein expressionProtein mutantsTransient expressionVirus buddingNonpermissive temperatureDomain sequencesMutantsCell surfaceGlycoprotein mutantsProteinImmunogold labelingSucrose gradientsEfficient assembly
1988
Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum.
Shaw A, Rottier P, Rose J. Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 7592-7596. PMID: 2845415, PMCID: PMC282238, DOI: 10.1073/pnas.85.20.7592.Peer-Reviewed Original ResearchConceptsSignal sequenceEndoplasmic reticulumC-terminal transmembraneType II transmembrane proteinInsertion of proteinsCleaved signal sequenceSignal sequence functionN-terminal extensionShort hydrophobic domainVesicular stomatitis virus glycoproteinMembrane anchorMutant proteinsCytoplasmic domainMembrane insertionTransmembrane proteinC-terminusCytoplasmic sideN-terminusBlock cleavageHydrophobic domainCleavage siteHeLa cellsPoint mutationsProteinMicrosomal membranesDifferential 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 surfaceEctodomainProteinFoldingEffects of altered cytoplasmic domains on transport of the vesicular stomatitis virus glycoprotein are transferable to other proteins.
Guan J, Ruusala A, Cao H, Rose J. Effects of altered cytoplasmic domains on transport of the vesicular stomatitis virus glycoprotein are transferable to other proteins. Molecular And Cellular Biology 1988, 8: 2869-2874. PMID: 2841589, PMCID: PMC363506, DOI: 10.1128/mcb.8.7.2869.Peer-Reviewed Original ResearchConceptsVesicular stomatitis virus glycoproteinEndoplasmic reticulumCytoplasmic domainVesicular stomatitis virus G proteinMembrane-anchored formVirus G proteinVirus glycoproteinMutant proteinsProtein foldingCytoplasmic sideSecretory proteinsCytoplasmic mutationsG proteinsProteinReticulumDifferent assaysMonomeric structureDetectable effectMutationsSedimentation coefficientRecent studiesEffects of Altered Cytoplasmic Domains on Transport of the Vesicular Stomatitis Virus Glycoprotein Are Transferable to Other Proteins
Guan J, Ruusala A, Cao H, Rose J. Effects of Altered Cytoplasmic Domains on Transport of the Vesicular Stomatitis Virus Glycoprotein Are Transferable to Other Proteins. Molecular And Cellular Biology 1988, 8: 2869-2874. DOI: 10.1128/mcb.8.7.2869-2874.1988.Peer-Reviewed Original ResearchVesicular stomatitis virus glycoproteinEndoplasmic reticulumCytoplasmic domainVesicular stomatitis virus G proteinHuman chorionic gonadotropinMembrane-anchored formVirus G proteinVirus glycoproteinMutant proteinsProtein foldingChorionic gonadotropinCytoplasmic mutationsCytoplasmic sideSecretory proteinsG proteinsProteinDifferent assaysReticulumCell-surface expression of a membrane-anchored form of the human chorionic gonadotropin alpha subunit.
Guan J, Cao H, Rose J. Cell-surface expression of a membrane-anchored form of the human chorionic gonadotropin alpha subunit. Journal Of Biological Chemistry 1988, 263: 5306-5313. PMID: 2451667, DOI: 10.1016/s0021-9258(18)60716-1.Peer-Reviewed Original ResearchMeSH KeywordsBiological Transport, ActiveCloning, MolecularDNAElectrophoresis, Polyacrylamide GelFluorescent Antibody TechniqueGene Expression RegulationGlycoprotein Hormones, alpha SubunitGlycoside HydrolasesGlycosylationHexosaminidasesHumansKineticsMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMembranesOligosaccharidesPituitary Hormones, AnteriorPlasmidsTunicamycinVesicular stomatitis Indiana virusViral Fusion ProteinsConceptsVesicular stomatitis virus glycoproteinAsparagine-linked glycansAnimal cellsAlpha subunitNovel cell surface proteinCarboxyl-terminal amino acidsGlycosylation inhibitor tunicamycinAbsence of glycosylationMembrane-anchored formCell surface proteinsSecond glycosylation siteHuman chorionic gonadotropin (hCG) alpha-subunitVirus glycoproteinEntire precursorCell surface expressionCytoplasmic domainGonadotropin alpha subunitHybrid proteinPlasma membraneGlycosylation sitesSecretory proteinsCellular membranesConformational changesCell surfaceAmino acids