2001
Quality control of transmembrane domain assembly in the tetraspanin CD82
Cannon K, Cresswell P. Quality control of transmembrane domain assembly in the tetraspanin CD82. The EMBO Journal 2001, 20: 2443-2453. PMID: 11350933, PMCID: PMC125455, DOI: 10.1093/emboj/20.10.2443.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumTransmembrane segmentsDomain assemblyER quality controlFirst transmembrane segmentMore transmembrane segmentsER membraneER lumenChaperone calnexinSeparate polypeptidesTetraspanin CD82TM-1Extracellular domainCalnexinNative structureCell surfaceTM-2Lipid bilayersCD82AssemblyQuality controlPrimary mechanismProlonged interactionPolypeptideCalreticulinGlycosylation and the Immune System
Rudd P, Elliott T, Cresswell P, Wilson I, Dwek R. Glycosylation and the Immune System. Science 2001, 291: 2370-2376. PMID: 11269318, DOI: 10.1126/science.291.5512.2370.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigen PresentationAntigen-Antibody ReactionsAntigen-Presenting CellsAntigens, CD1Carrier ProteinsCollectinsComplement System ProteinsEndoplasmic ReticulumEpitopesGlycoproteinsGlycosylationHistocompatibility AntigensHumansImmune SystemImmunoglobulinsPolysaccharidesProtein FoldingT-LymphocytesViral Envelope ProteinsConceptsImmune systemMajor histocompatibility complex antigensAntigen-presenting cellsAdaptive immune responsesCellular immune systemHistocompatibility complex antigensHumoral immune systemT cell receptor complexRheumatoid arthritisMannose-binding lectinAutoimmune diseasesCell receptor complexT cellsImmune responseComplex antigensPeptide antigensComplement componentsImmunoglobulin GAntigenKey moleculesReceptor complexSpecific glycoformsGlycoproteinGlycopeptide antigensArthritisA 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
2000
Intracellular Surveillance: Controlling the Assembly of MHC Class I‐Peptide Complexes
Cresswell P. Intracellular Surveillance: Controlling the Assembly of MHC Class I‐Peptide Complexes. Traffic 2000, 1: 301-305. PMID: 11208114, DOI: 10.1034/j.1600-0854.2000.010402.x.Peer-Reviewed Original Research
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, Quaternary
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 moleculesHeterodimersAssembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors.
Deng Y, Gibbs J, Bačík I, Porgador A, Copeman J, Lehner P, Ortmann B, Cresswell P, Bennink J, Yewdell J. Assembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors. The Journal Of Immunology 1998, 161: 1677-85. PMID: 9712031, DOI: 10.4049/jimmunol.161.4.1677.Peer-Reviewed Original ResearchMeSH KeywordsAedesAnimalsAntibodies, MonoclonalAntiportersCell LineEndoplasmic ReticulumH-2 AntigensHeLa CellsHumansImmunoglobulinsLymphocyte ActivationMacromolecular SubstancesMembrane Transport ProteinsMiceOligopeptidesOvalbuminPeptide FragmentsProtease InhibitorsRecombinant ProteinsT-LymphocytesVaccinia virusConceptsInsect cellsEndoplasmic reticulumVertebrate cellsHuman cellsHuman tapasinVaccinia virus-mediated expressionCell surface expressionProtease inhibitorsInefficient assemblyKbMHC class IMouse betaInsectsEfficient assemblyImmediate precursorSurface expressionAntigenic peptidesHeavy chainClass IRecombinant vaccinia virusVirus-mediated expressionAssemblyExpressionCellsVaccinia virusThe 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-IsomerasesRibonucleoproteinsMECHANISMS OF MHC CLASS I–RESTRICTED ANTIGEN PROCESSING
Pamer E, Cresswell P. MECHANISMS OF MHC CLASS I–RESTRICTED ANTIGEN PROCESSING. Annual Review Of Immunology 1998, 16: 323-358. PMID: 9597133, DOI: 10.1146/annurev.immunol.16.1.323.Peer-Reviewed Original ResearchSoluble 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
Protein degradation: The ins and outs of the matter
Cresswell P, Hughes E. Protein degradation: The ins and outs of the matter. Current Biology 1997, 7: r552-r555. PMID: 9285707, DOI: 10.1016/s0960-9822(06)00279-x.Peer-Reviewed Original ResearchA 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, CulturedMisfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome
Hughes E, Hammond C, Cresswell P. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 1896-1901. PMID: 9050876, PMCID: PMC20014, DOI: 10.1073/pnas.94.5.1896.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcysteineBeta 2-MicroglobulinBlotting, WesternCysteine EndopeptidasesCysteine Proteinase InhibitorsCytoplasmEndoplasmic ReticulumEnzyme InhibitorsGlycosylationHistocompatibility Antigens Class IHumansKineticsLeupeptinsMultienzyme ComplexesProteasome Endopeptidase ComplexProtein FoldingSolubilityTransfectionTumor Cells, CulturedConceptsClass I heavy chainsMHC class I heavy chainMajor histocompatibility complex class I heavy chainsBeta2-microglobulinHeavy chainMHC class ICell linesCell line DaudiTAP-deficient cell linesSpecific irreversible inhibitorClass IHerpes simplex virus proteinDaudiVirus proteinsEndoplasmic reticulumIrreversible inhibitorSimilar accumulationLactacystinPeriod of hours
1996
Processing 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
1994
MHC 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