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A novel cytosolic class I antigen-processing pathway for endoplasmic-reticulum-targeted proteins.
EMBO Rep. 8, 945-951 (2007)
Proteins bearing an endoplasmic reticulum (ER) leader are inserted into the ER followed by cleavage of the signal peptide. Major histocompatibility complex class I-restricted T-cell epitopes can be generated from these proteins by the proteasome after retrotranslocation into the cytosol. Here, we show that an HLA-A*0201-restricted epitope from prostate stem cell antigen contains the cleavage site of the ER signal peptidase. The resulting cleavage products fail to bind to HLA-A*0201 and are not recognized by T lymphocytes. As processing of prostate stem cell antigen by signal peptidase occurs immediately after co-translational insertion, the epitope must be processed from polypeptides that have never reached the ER. The processing of this epitope depends on the proteasome and the transporter associated with antigen processing and shows a novel pathway of class I processing that relies on the failure of ER-targeted proteins to reach their target compartment.
Impact Factor
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Times Cited
Times Cited
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Cited By
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8.175
0.000
11
11
Anmerkungen
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
endoplasmic reticulum; antigen processing; Major histocompatibility complex class I; signal peptidase; cytoxic T lymphocytes
Sprache
englisch
Veröffentlichungsjahr
2007
HGF-Berichtsjahr
2007
ISSN (print) / ISBN
1469-221X
e-ISSN
1469-3178
Zeitschrift
EMBO Reports
Quellenangaben
Band: 8,
Heft: 10,
Seiten: 945-951
Verlag
EMBO Press
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Virology (VIRO)
POF Topic(s)
30203 - Molecular Targets and Therapies
Forschungsfeld(er)
Immune Response and Infection
PSP-Element(e)
G-502700-002
PubMed ID
17404459
WOS ID
000249884600015
Scopus ID
34848897897
Erfassungsdatum
2007-11-09