ERAAP synergizes with MHC class I molecules to make the final cut in the antigenic peptide precursors in the endoplasmic reticulum.

Journal Article (Journal Article)

The major histocompatibility complex class I molecules display peptides (pMHC I) on the cell surface for immune surveillance by CD8(+) T cells. These peptides are generated by proteolysis of intracellular polypeptides by the proteasome in the cytoplasm and then in the endoplasmic reticulum (ER) by the ER aminopeptidase associated with antigen processing (ERAAP). To define the unknown mechanism of ERAAP function in vivo, we analyzed naturally processed peptides in cells with or without appropriate MHC I and ERAAP. In the absence of MHC I, ERAAP degraded the antigenic precursors in the ER. However, MHC I molecules could bind proteolytic intermediates and were essential for generation of the final peptide by ERAAP. Thus, ERAAP synergizes with MHC I to generate the final pMHC I repertoire.

Full Text

Duke Authors

Cited Authors

  • Kanaseki, T; Blanchard, N; Hammer, GE; Gonzalez, F; Shastri, N

Published Date

  • November 2006

Published In

Volume / Issue

  • 25 / 5

Start / End Page

  • 795 - 806

PubMed ID

  • 17088086

Pubmed Central ID

  • PMC2746443

International Standard Serial Number (ISSN)

  • 1074-7613

Digital Object Identifier (DOI)

  • 10.1016/j.immuni.2006.09.012


  • eng

Conference Location

  • United States