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Mol Immunol. 2016 Jan;69:99-105. doi: 10.1016/j.molimm.2015.11.004. Epub 2015 Nov 17.

Chaperone BAG6 is dispensable for MHC class I antigen processing and presentation.

Author information

1
Division of Immunology, Department of Biology, University of Konstanz, D-78457 Konstanz, Germany.
2
Division of Immunology, Department of Biology, University of Konstanz, D-78457 Konstanz, Germany; Biotechnology Institute Thurgau (BITg) at the University of Konstanz, CH-8280 Kreuzlingen, Switzerland.
3
Division of Immunology, Department of Biology, University of Konstanz, D-78457 Konstanz, Germany; Biotechnology Institute Thurgau (BITg) at the University of Konstanz, CH-8280 Kreuzlingen, Switzerland. Electronic address: Marcus.Groettrup@uni-konstanz.de.

Abstract

Antigen processing for direct presentation on MHC class I molecules is a multistep process requiring the concerted activity of several cellular complexes. The essential steps at the beginning of this pathway, namely protein synthesis at the ribosome and degradation via the proteasome, have been known for years. Nevertheless, there is a considerable lack of factors identified to function between protein synthesis and degradation during antigen processing. Here, we analyzed the impact of the chaperone BAG6 on MHC class I cell surface expression and presentation of virus-derived peptides. Although an essential role of BAG6 in antigen processing has been proposed previously, we found BAG6 to be dispensable in this pathway. Still, interaction of BAG6 and the model antigen tyrosinase was enhanced during proteasome inhibition pointing towards a role of BAG6 in antigen degradation. Redundant chaperone pathways potentially mask the contribution of BAG6 to antigen processing and presentation.

KEYWORDS:

Antigen presentation; Antigen processing; BAG6; DRiPs; MHC class I

PMID:
26598275
DOI:
10.1016/j.molimm.2015.11.004
[Indexed for MEDLINE]

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