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• W2951112518 abstract "Abstract Tapasin and TAPBPR are known to perform peptide editing on major histocompatibility complex class I (MHC I) molecules, however, the precise molecular mechanism(s) involved in this process remain largely enigmatic. Here, using immunopeptidomics in combination with novel cell-based assays that assess TAPBPR-mediate peptide exchange, we reveal a critical role for the K22-D35 loop of TAPBPR in mediating peptide exchange on MHC I. We identify a specific leucine within this loop that enables TAPBPR to facilitate peptide dissociation from MHC I. Moreover, we delineate the molecular features of the MHC I F pocket required for TAPBPR to promote peptide dissociation in a loop-dependent manner. These data reveal that chaperone-mediated peptide editing of MHC I can occur by different mechanisms dependent on the C-terminal residue that the MHC I accommodates in its F pocket and provide novel insights that may inform the therapeutic potential of TAPBPR manipulation to increase tumour immunogenicity. Impact Statement This work demonstrates for the first time that the K22-D35 loop of TAPBPR is the essential region for mediating peptide exchange and peptide selection on major histocompatibility complex class I molecules." @default.
• W2951112518 created "2019-06-27" @default.
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• W2951112518 date "2018-11-05" @default.
• W2951112518 modified "2023-10-16" @default.
• W2951112518 title "TAPBPR mediates peptide dissociation from MHC class I using a leucine lever" @default.
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• W2951112518 doi "https://doi.org/10.1101/462432" @default.
• W2951112518 hasPublicationYear "2018" @default.
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