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

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Molecular Immunology ; 69 (2016). - S. 99-105. - ISSN 0161-5890. - eISSN 1872-9142
Zusammenfassung
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.
Zusammenfassung in einer weiteren Sprache
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570 Biowissenschaften, Biologie
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BAG6, Antigen processing, Antigen presentation, MHC class I, DRiPs
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Zitieren
ISO 690BITZER, Annegret, Michael BASLER, Marcus GRÖTTRUP, 2016. Chaperone BAG6 is dispensable for MHC class I antigen processing and presentation. In: Molecular Immunology. 69, pp. 99-105. ISSN 0161-5890. eISSN 1872-9142. Available under: doi: 10.1016/j.molimm.2015.11.004
BibTex
@article{Bitzer2016Chape-33604,
  year={2016},
  doi={10.1016/j.molimm.2015.11.004},
  title={Chaperone BAG6 is dispensable for MHC class I antigen processing and presentation},
  volume={69},
  issn={0161-5890},
  journal={Molecular Immunology},
  pages={99--105},
  author={Bitzer, Annegret and Basler, Michael and Gröttrup, Marcus}
}
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