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

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          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.

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          Author and article information

          Journal
          Mol. Immunol.
          Molecular immunology
          Elsevier BV
          1872-9142
          0161-5890
          Jan 2016
          : 69
          Affiliations
          [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.
          Article
          S0161-5890(15)30114-0
          10.1016/j.molimm.2015.11.004
          26598275

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