| First Author | Shen XZ | Year | 2011 |
| Journal | Nat Immunol | Volume | 12 |
| Issue | 11 | Pages | 1078-85 |
| PubMed ID | 21964607 | Mgi Jnum | J:177664 |
| Mgi Id | MGI:5295804 | Doi | 10.1038/ni.2107 |
| Citation | Shen XZ, et al. (2011) The carboxypeptidase ACE shapes the MHC class I peptide repertoire. Nat Immunol 12(11):1078-85 |
| abstractText | The surface presentation of peptides by major histocompatibility complex (MHC) class I molecules is critical to CD8(+) T cell-mediated adaptive immune responses. Aminopeptidases have been linked to the editing of peptides for MHC class I loading, but carboxy-terminal editing is thought to be due to proteasome cleavage. By analysis of wild-type mice and mice genetically deficient in or overexpressing the dipeptidase angiotensin-converting enzyme (ACE), we have now identified ACE as having a physiological role in the processing of peptides for MHC class I. ACE edited the carboxyl terminus of proteasome-produced MHC class I peptides. The lack of ACE exposed new antigens but also abrogated some self antigens. ACE had substantial effects on the surface expression of MHC class I in a haplotype-dependent manner. We propose a revised model of peptide processing for MHC class I by introducing carboxypeptidase activity into the process. |
