2001
Distinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP)
Karttunen J, Lehner P, Gupta S, Hewitt E, Cresswell P. Distinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP). Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 7431-7436. PMID: 11381133, PMCID: PMC34686, DOI: 10.1073/pnas.121180198.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SubstitutionAnimalsATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersAzidesBinding SitesCell LineHeLa CellsHumansLysineMajor Histocompatibility ComplexMutagenesis, Site-DirectedPeptide FragmentsPhotoaffinity LabelsProtein SubunitsRecombinant ProteinsTransfectionA Role for Calnexin in the Assembly of the MHC Class I Loading Complex in the Endoplasmic Reticulum
Diedrich G, Bangia N, Pan M, Cresswell P. A Role for Calnexin in the Assembly of the MHC Class I Loading Complex in the Endoplasmic Reticulum. The Journal Of Immunology 2001, 166: 1703-1709. PMID: 11160214, DOI: 10.4049/jimmunol.166.3.1703.Peer-Reviewed Original ResearchAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersCalcium-Binding ProteinsCalnexinCalreticulinCell Line, TransformedDimerizationEndoplasmic ReticulumHeat-Shock ProteinsHeLa CellsHistocompatibility Antigens Class IHLA AntigensHumansImmunoglobulinsIsomerasesKineticsMajor Histocompatibility ComplexMembrane Transport ProteinsProtein BindingProtein Disulfide-IsomerasesRibonucleoproteinsTumor Cells, Cultured
1999
The nature of the MHC class I peptide loading complex
Cresswell P, Bangia N, Dick T, Diedrich G. The nature of the MHC class I peptide loading complex. Immunological Reviews 1999, 172: 21-28. PMID: 10631934, DOI: 10.1111/j.1600-065x.1999.tb01353.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigen PresentationATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersDimerizationEndoplasmic ReticulumHistocompatibility Antigens Class IHumansModels, MolecularPeptidesProtein BindingProtein Structure, QuaternaryThe N‐terminal region of tapasin is required to stabilize the MHC class I loading complex
Bangia N, Lehner P, Hughes E, Surman M, Cresswell P. The N‐terminal region of tapasin is required to stabilize the MHC class I loading complex. European Journal Of Immunology 1999, 29: 1858-1870. PMID: 10382748, DOI: 10.1002/(sici)1521-4141(199906)29:06<1858::aid-immu1858>3.0.co;2-c.Peer-Reviewed Original ResearchAntigen PresentationAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBase SequenceBeta 2-MicroglobulinBinding SitesBiological Transport, ActiveCalcium-Binding ProteinsCalreticulinCell LineDNA PrimersDrug StabilityHeat-Shock ProteinsHistocompatibility Antigens Class IHumansImmunoglobulinsIsomerasesKineticsMacromolecular SubstancesMembrane Transport ProteinsMolecular ChaperonesProtein BindingProtein Disulfide-IsomerasesRibonucleoproteins
1998
Elucidation of the genetic basis of the antigen presentation defects in the mutant cell line .220 reveals polymorphism and alternative splicing of the tapasin gene
Copeman J, Bangia N, Cross J, Cresswell P. Elucidation of the genetic basis of the antigen presentation defects in the mutant cell line .220 reveals polymorphism and alternative splicing of the tapasin gene. European Journal Of Immunology 1998, 28: 3783-3791. PMID: 9842921, DOI: 10.1002/(sici)1521-4141(199811)28:11<3783::aid-immu3783>3.0.co;2-9.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAntigen PresentationAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersB-LymphocytesCell LineDNA, ComplementaryEndoplasmic ReticulumExonsHumansImmunoglobulinsMembrane Transport ProteinsMutationPolymorphism, GeneticReverse Transcriptase Polymerase Chain ReactionConceptsMutant cell linesEndoplasmic reticulumAlternative splicingN-terminal 49 amino acidsGenetic basisTapasin geneExon twoWild-type cellsFull-length transcriptsCell linesSingle nucleotide substitutionSignal peptideSecond intronNucleotide substitutionsPhysical associationSplice siteGlycoprotein tapasinPosition 240Amino acidsClass I moleculesSplicingOptimal bindingGenesI moleculesHeterodimersThe thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex
Hughes E, Cresswell P. The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex. Current Biology 1998, 8: 709-713. PMID: 9637923, DOI: 10.1016/s0960-9822(98)70278-7.Peer-Reviewed Original ResearchAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersCalcium-Binding ProteinsCalreticulinEndoplasmic ReticulumHeat-Shock ProteinsHeLa CellsHistocompatibility Antigens Class IHumansImmunoglobulinsIsomerasesMembrane Transport ProteinsPeptidesProtein Disulfide Reductase (Glutathione)Protein Disulfide-IsomerasesRibonucleoproteinsHLA-B27–Restricted Antigen Presentation in the Absence of Tapasin Reveals Polymorphism in Mechanisms of HLA Class I Peptide Loading
Peh C, Burrows S, Barnden M, Khanna R, Cresswell P, Moss D, McCluskey J. HLA-B27–Restricted Antigen Presentation in the Absence of Tapasin Reveals Polymorphism in Mechanisms of HLA Class I Peptide Loading. Immunity 1998, 8: 531-542. PMID: 9620674, DOI: 10.1016/s1074-7613(00)80558-0.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAnimalsAntigen PresentationAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersBeta 2-MicroglobulinCells, CulturedDisease SusceptibilityHLA-B AntigensHLA-B27 AntigenHLA-B44 AntigenHumansImmunoglobulinsMembrane Transport ProteinsMicePolymorphism, GeneticProtein BindingSurface PropertiesTransfectionCalnexin expression does not enhance the generation of MHC class I‐peptide complexes
Prasad S, Yewdell J, Porgador A, Sadasivan B, Cresswell P, Bennink J. Calnexin expression does not enhance the generation of MHC class I‐peptide complexes. European Journal Of Immunology 1998, 28: 907-913. PMID: 9541586, DOI: 10.1002/(sici)1521-4141(199803)28:03<907::aid-immu907>3.0.co;2-4.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, ViralATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBeta 2-MicroglobulinBiological TransportCalcium-Binding ProteinsCalnexinCell CompartmentationCells, CulturedH-2 AntigensHistocompatibility Antigens Class IHumansMacromolecular SubstancesMiceOvalbuminPeptidesProtein BindingGenomic analysis of the Tapasin gene, located close to the TAP loci in the MHC
Herberg J, Sgouros J, Jones T, Copeman J, Humphray S, Sheer D, Cresswell P, Beck S, Trowsdale J. Genomic analysis of the Tapasin gene, located close to the TAP loci in the MHC. European Journal Of Immunology 1998, 28: 459-467. PMID: 9521053, DOI: 10.1002/(sici)1521-4141(199802)28:02<459::aid-immu459>3.0.co;2-z.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBase SequenceCentromereExonsGenes, MHC Class IHistocompatibility Antigens Class IHumansImmunoglobulinsIntronsMembrane Transport ProteinsMiceMolecular Sequence DataPhylogenyRatsConceptsTapasin geneMouse ESTsSyntenic positionsGenomic analysisSeparate exonsGene sequencesDistinct phylogenyEndoplasmic reticulumGenesK locusChromosome 17IgC domainFunctional significanceLociMHC class IClass IHLA-DP locusTAP2 genesEquivalent locationsTAP transporterTapasin moleculePhylogenyIntronsChromosomesESTsSoluble Tapasin Restores MHC Class I Expression and Function in the Tapasin-Negative Cell Line .220
Lehner P, Surman M, Cresswell P. Soluble Tapasin Restores MHC Class I Expression and Function in the Tapasin-Negative Cell Line .220. Immunity 1998, 8: 221-231. PMID: 9492003, DOI: 10.1016/s1074-7613(00)80474-4.Peer-Reviewed Original ResearchAntigen PresentationAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersBiological TransportEndoplasmic ReticulumHLA-B8 AntigenHumansImmunoglobulinsMembrane Transport ProteinsMutationPeptidesProtein BindingSolubilityT-Lymphocytes, Cytotoxic
1997
A Critical Role for Tapasin in the Assembly and Function of Multimeric MHC Class I-TAP Complexes
Ortmann B, Copeman J, Lehner P, Sadasivan B, Herberg J, Grandea A, Riddell S, Tampé R, Spies T, Trowsdale J, Cresswell P. A Critical Role for Tapasin in the Assembly and Function of Multimeric MHC Class I-TAP Complexes. Science 1997, 277: 1306-1309. PMID: 9271576, DOI: 10.1126/science.277.5330.1306.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigen PresentationAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersCalcium-Binding ProteinsCalreticulinCell LineCell Line, TransformedChromosome MappingChromosomes, Human, Pair 6Cloning, MolecularDimerizationEndoplasmic ReticulumGenetic LinkageHistocompatibility Antigens Class IHLA AntigensHumansImmunoglobulin GImmunoglobulinsMajor Histocompatibility ComplexMembrane Transport ProteinsMolecular Sequence DataRibonucleoproteinsSequence Homology, Amino AcidT-Lymphocytes, CytotoxicTumor Cells, CulturedInterferon-γ Rapidly Increases Peptide Transporter (TAP) Subunit Expression and Peptide Transport Capacity in Endothelial Cells*
Ma W, Pober J, Johnson D, Lehner P, Cresswell P. Interferon-γ Rapidly Increases Peptide Transporter (TAP) Subunit Expression and Peptide Transport Capacity in Endothelial Cells*. Journal Of Biological Chemistry 1997, 272: 16585-16590. PMID: 9195970, DOI: 10.1074/jbc.272.26.16585.Peer-Reviewed Original Research
1996
Roles for Calreticulin and a Novel Glycoprotein, Tapasin, in the Interaction of MHC Class I Molecules with TAP
Sadasivan B, Lehner P, Ortmann B, Spies T, Cresswell P. Roles for Calreticulin and a Novel Glycoprotein, Tapasin, in the Interaction of MHC Class I Molecules with TAP. Immunity 1996, 5: 103-114. PMID: 8769474, DOI: 10.1016/s1074-7613(00)80487-2.Peer-Reviewed Original ResearchATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBeta 2-MicroglobulinCalcium-Binding ProteinsCalreticulinCell LineGlycoproteinsHistocompatibility Antigens Class IHLA-A AntigensHLA-B AntigensHLA-C AntigensHumansIndolizinesMolecular ChaperonesMutationPeptidesRibonucleoproteinsProcessing and delivery of peptides presented by MHC class I molecules
Lehner P, Cresswell P. Processing and delivery of peptides presented by MHC class I molecules. Current Opinion In Immunology 1996, 8: 59-67. PMID: 8729447, DOI: 10.1016/s0952-7915(96)80106-3.Peer-Reviewed Original ResearchAnimalsAntigen PresentationATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersCysteine EndopeptidasesCytotoxicity, ImmunologicEndoplasmic ReticulumEpitopesHistocompatibility Antigens Class IHumansInterferon-gammaMiceMice, KnockoutModels, MolecularMultienzyme ComplexesProteasome Endopeptidase Complex
1995
Assembly, Intracellular Localization, and Nucleotide Binding Properties of the Human Peptide Transporters TAP1 and TAP2 Expressed by Recombinant Vaccinia Viruses (∗)
Russ G, Esquivel F, Yewdell J, Cresswell P, Spies T, Bennink J. Assembly, Intracellular Localization, and Nucleotide Binding Properties of the Human Peptide Transporters TAP1 and TAP2 Expressed by Recombinant Vaccinia Viruses (∗). Journal Of Biological Chemistry 1995, 270: 21312-21318. PMID: 7673167, DOI: 10.1074/jbc.270.36.21312.Peer-Reviewed Original ResearchMeSH KeywordsATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersCell LineDetergentsFluorescent Antibody TechniqueGlycosylationHumansMajor Histocompatibility ComplexMicroscopy, ConfocalNucleotidesProtein BindingRecombination, GeneticVaccinia virus
1994
Human transporters associated with antigen processing possess a promiscuous peptide-binding site
Androlewicz M, Cresswell P. Human transporters associated with antigen processing possess a promiscuous peptide-binding site. Immunity 1994, 1: 7-14. PMID: 7889401, DOI: 10.1016/1074-7613(94)90004-3.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceAntigen PresentationATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBinding SitesBinding, CompetitiveBiological Transport, ActiveCarrier ProteinsCell LineHistocompatibility Antigens Class IHumansMolecular Sequence DataOligopeptidesMHC class l/β2-microglobulin complexes associate with TAP transporters before peptide binding
Ortmann B, Androlewicz M, Cresswell P. MHC class l/β2-microglobulin complexes associate with TAP transporters before peptide binding. Nature 1994, 368: 864-867. PMID: 8159247, DOI: 10.1038/368864a0.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersBeta 2-MicroglobulinBiological TransportB-LymphocytesCalcium-Binding ProteinsCalnexinCarrier ProteinsCell LineDigitoninEndoplasmic ReticulumHistocompatibility Antigens Class IHLA-A3 AntigenHumansMiceMolecular Sequence DataProtein BindingRabbitsSolubility
1992
Proteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I molecules
Arnold D, Driscoll J, Androlewicz M, Hughes E, Cresswell P, Spies T. Proteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I molecules. Nature 1992, 360: 171-174. PMID: 1436094, DOI: 10.1038/360171a0.Peer-Reviewed Original ResearchAntigen-Antibody ReactionsAntigens, ViralATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersCarrier ProteinsCell LineChromatography, High Pressure LiquidCysteine EndopeptidasesElectrophoresis, Gel, Two-DimensionalHistocompatibility Antigens Class IHistocompatibility Antigens Class IIHLA-A AntigensHLA-B AntigensHumansMembrane ProteinsMultienzyme ComplexesProteasome Endopeptidase ComplexProteinsT-LymphocytesTransfectionViral Matrix Proteins