| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 3354146 | Immunity | 2007 | 10 Pages |
Abstract
SummaryMajor histocompatibility complex (MHC) class I molecules present short, perfectly cleaved peptides on the cell surface for immune surveillance by CD8+ T cells. The pathway for generating these peptides begins in the cytoplasm, and the peptide-MHC I (pMHC I) repertoire is finalized in the endoplasmic reticulum. Recent studies show that the peptides for MHC I are customized by the ER aminopeptidase associated with antigen processing and by dynamic interactions within the MHC peptide-loading complex. Failure to customize the pMHC I repertoire has profound immunological consequences.
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Authors
Gianna Elena Hammer, Takayuki Kanaseki, Nilabh Shastri,