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• W2062908727 startingPage "467" @default.
• W2062908727 abstract "MHC class I ligands are produced mainly by proteasomal proteolysis, in conjunction with an unknown extent of trimming by peptidases. Trimming of precursor peptides in the endoplasmic reticulum, a process postulated to be class I dependent, may substantially enhance the efficiency of antigen presentation. However, monitoring of luminal peptide processing has not so far been possible. Here we show that several precursor peptides with amino-terminal extensions are rapidly converted to HLA-A2 ligands by one or several highly efficient metallo-peptidases found on the outer surface of, but also within, microsomes. Surprisingly, luminal trimming is fully active in HLA class I- or TAP-deficient microsomes and precedes peptide association with HLA class I molecules. Trimmed peptides are rapidly depleted from, and become undetectable in, microsomes lacking the restricting class I molecules." @default.
• W2062908727 created "2016-06-24" @default.
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• W2062908727 date "2001-09-01" @default.
• W2062908727 modified "2023-10-10" @default.
• W2062908727 title "Efficient MHC Class I-Independent Amino-Terminal Trimming of Epitope Precursor Peptides in the Endoplasmic Reticulum" @default.
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• W2062908727 doi "https://doi.org/10.1016/s1074-7613(01)00203-5" @default.
• W2062908727 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11567636" @default.
• W2062908727 hasPublicationYear "2001" @default.
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