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•], this paper reports the molecular cloning of human tapasin. The stoichiometry of TAP, tapasin and MHC class I molecules in peptide-loading complexes is also analysed.
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Two novel functions for tapasin are described here. Full-length tapasin increases TAP levels and thereby peptide translocation into the ER; moreover, soluble tapasin restores class I cell-surface expression without binding TAP. Stabilisation of empty class I dimers or their peptide-binding sites and peptide editing are discussed as explanations for the latter phenomenon.
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The authors show that a peptide forming unstable complexes with MHC class I dissociates more rapidly from class I molecules when these are retained in the ER. This suggests a mechanism for optimisation or 'editing' of class-I-bound peptides in the ER.
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This is a study of intracellular peptide assembly of three HLA class I molecules in 721.220 cells; it reveals a surprisingly efficient (but as yet unexplained) peptide assembly of HLA-B27 in the absence of tapasin, as compared to HLA-B8 or -B44.
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Using photoreactive peptides, three ER proteins and one protein (other than TAP) on the cytosolic face of murine microsomes are shown to bind peptides. Increased peptide binding to p100, the membrane-associated protein on the cytosolic face of the ER, may be secondary to a defect in the TAP-related antigen processing pathway.
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Marusina K, Reid G, Gabathuler R, Jefferies W, Monaco JJ Novel peptide-binding proteins and peptide transport in normal and TAP-deficient microsomes. Biochemistry. 36:1997;856-863. Using photoreactive peptides, three ER proteins and one protein (other than TAP) on the cytosolic face of murine microsomes are shown to bind peptides. Increased peptide binding to p100, the membrane-associated protein on the cytosolic face of the ER, may be secondary to a defect in the TAP-related antigen processing pathway.
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Starting from the phenomenon of polymorphic presentation of a minor histocompatibility antigen epitope in HLA-B27-transgenic rats and mice, the authors map the responsible locus (cim2) to a ~50-75 kilobase region in the centromeric MHC complex of the mouse. Cim2 is distinct from TAP, LMP and tapasin and has a broad effect on peptide presentation by HLA-B27 and two murine MHC class I molecules.
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Simmons WA, Roopenian DC, Summerfield SG, Jones RC, Galocha B, Christianson GJ, Maika SD, Zhou M, Gaskell SJ, Bordoli RSet al. A new MHC locus that influences class I peptide presentation. Immunity. 7:1997;641-651. Starting from the phenomenon of polymorphic presentation of a minor histocompatibility antigen epitope in HLA-B27-transgenic rats and mice, the authors map the responsible locus (cim2) to a ~50-75 kilobase region in the centromeric MHC complex of the mouse. Cim2 is distinct from TAP, LMP and tapasin and has a broad effect on peptide presentation by HLA-B27 and two murine MHC class I molecules.
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