Abstract
Abstract Signal sequences of human MHC class I molecules are a unique source of epitopes for newly synthesized nonclassical HLA-E molecules. Binding of such conserved peptides to HLA-E induces its cell surface expression and protects cells from NK cell attack. After cleavage from the pre-protein, we show that the liberated MHC class I signal peptide is further processed by signal peptide peptidase in the hydrophobic, membrane-spanning region. This cut is essential for the release of the HLA-E epitope-containing fragment from the lipid bilayer and its subsequent transport into the lumen of the endoplasmic reticulum via the TAP.
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Dates
Type | When |
---|---|
Created | 11 years, 4 months ago (April 20, 2014, 8:08 p.m.) |
Deposited | 8 months ago (Jan. 2, 2025, 12:19 p.m.) |
Indexed | 3 months ago (June 3, 2025, 5:03 a.m.) |
Issued | 23 years, 9 months ago (Dec. 1, 2001) |
Published | 23 years, 9 months ago (Dec. 1, 2001) |
Published Print | 23 years, 9 months ago (Dec. 1, 2001) |
@article{Lemberg_2001, title={Intramembrane Proteolysis of Signal Peptides: An Essential Step in the Generation of HLA-E Epitopes}, volume={167}, ISSN={1550-6606}, url={http://dx.doi.org/10.4049/jimmunol.167.11.6441}, DOI={10.4049/jimmunol.167.11.6441}, number={11}, journal={The Journal of Immunology}, publisher={Oxford University Press (OUP)}, author={Lemberg, Marius K. and Bland, Felicity A. and Weihofen, Andreas and Braud, Veronique M. and Martoglio, Bruno}, year={2001}, month=dec, pages={6441–6446} }