Essential glycan-dependent interactions optimize MHC class I peptide loading
作者： P. A. Wearsch , D. R. Peaper , P. Cresswell
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摘要: In this study we sought to better understand the role of glycoprotein quality control machinery in assembly MHC class I molecules with high-affinity peptides. The lectin-like chaperone calreticulin (CRT) and thiol oxidoreductase ERp57 participate final step process as part peptide-loading complex (PLC). We provide evidence for an I/CRT intermediate before PLC engagement examine nature that interaction detail. To investigate mechanism peptide loading roles individual components, reconstituted a subcomplex, excluding Transporter Associated Antigen Processing, from purified, recombinant proteins. disulfide linked I-specific tapasin CRT were minimal components required association loading. Mutations disrupting or glycan completely eliminated activity vitro. By using purified system, also direct UDP-glucose:glycoprotein glucosyltransferase 1 assembly. Drosophila enzyme reglucosylated associated suboptimal ligands allowed reengagement exchange. Collectively, data indicate enhances weak tapasin/class interactions manner is glycan-dependent regulated by 1.
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