Control of MHC Class I Traffic from the Endoplasmic Reticulum by Cellular Chaperones and Viral Anti‐Chaperones
MHC class I molecules assemble with peptides in the endoplasmic reticulum (ER). To ensure that only peptide‐loaded MHC molecules leave the ER, empty molecules are retained by ER‐resident chaperones, most notably the MHC‐specific tapasin. ER exit of class I MHC is also controlled by viruses, but for...
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Veröffentlicht in: | Traffic (Copenhagen, Denmark) Denmark), 2000-04, Vol.1 (4), p.306-311 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | MHC class I molecules assemble with peptides in the endoplasmic reticulum (ER). To ensure that only peptide‐loaded MHC molecules leave the ER, empty molecules are retained by ER‐resident chaperones, most notably the MHC‐specific tapasin. ER exit of class I MHC is also controlled by viruses, but for the opposite purpose of preventing peptide presentation to T cells. Interestingly, some viral proteins are able to retain MHC class I molecules in the ER despite being transported. By contrast, other viral proteins exit the ER only upon binding to class I MHC, thereby rerouting newly synthesized class I molecules to intracellular sites of proteolysis. Thus, immune escape can be achieved by reversing, inhibiting or redirecting the chaperone‐assisted MHC class I folding, assembly and intracellular transport. |
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ISSN: | 1398-9219 1600-0854 |
DOI: | 10.1034/j.1600-0854.2000.010403.x |