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- W2157525472 abstract "In contrast to the fairly well-characterized mechanism of assembly of MHC class I-peptide complexes, the disassembly mechanism by which peptide-loaded MHC class I molecules are released from the peptide-loading complex and exit the endoplasmic reticulum (ER) is poorly understood. Optimal peptide binding by MHC class I molecules is assumed to be sufficient for triggering exit of peptide-filled MHC class I molecules from the ER. We now show that protein disulfide isomerase (PDI) controls MHC class I disassembly by regulating dissociation of the tapasin-ERp57 disulfide conjugate. PDI acts as a peptide-dependent molecular switch; in the peptide-bound state, it binds to tapasin and ERp57 and induces dissociation of the tapasin-ERp57 conjugate. In the peptide-free state, PDI is incompetent to bind to tapasin or ERp57 and fails to dissociate the tapasin-ERp57 conjugates, resulting in ER retention of MHC class I molecules. Thus, our results indicate that even after optimal peptide loading, MHC class I disassembly does not occur by default but, rather, is a regulated process involving PDI-mediated interactions within the peptide-loading complex." @default.
- W2157525472 created "2016-06-24" @default.
- W2157525472 creator A5001514164 @default.
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- W2157525472 date "2009-07-15" @default.
- W2157525472 modified "2023-10-18" @default.
- W2157525472 title "Redox-regulated Export of the Major Histocompatibility Complex Class I-Peptide Complexes from the Endoplasmic Reticulum" @default.
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- W2157525472 doi "https://doi.org/10.1091/mbc.e09-03-0238" @default.
- W2157525472 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2710829" @default.
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