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The immunoproteasome in antigen processing and other immunological functions

Michael Basler1, Christopher J Kirk, Marcus Groettrup

  • 1Division of Immunology, Department of Biology, University of Konstanz, Universitätsstrasse 10, D-78457 Konstanz, Germany. Michael.Basler@uni-konstanz.de

Current Opinion in Immunology
|December 11, 2012
PubMed

Treatment of cells with interferon-γ leads to the replacement of the constitutive catalytic proteasome subunits β1, β2, and β5 by the inducible subunits LMP2 (β1i), MECL-1 (β2i), and LMP7 (β5i), respectively, building the so-called immunoproteasome. The incorporation of these subunits is required for the production of numerous MHC class-I restricted T cell epitopes. Recently, new evidence for an involvement of the immunoproteasome in other facets of the immune response emerged. Investigations of autoimmune diseases in animal models and a genetic predisposition of β5i in human autoimmune disorders suggest a crucial function of the immunoproteasome in proinflammatory diseases. The recent elucidation of the high-resolution structure of the immunoproteasome will facilitate the design of immunoproteasome selective inhibitors for pharmacological intervention.

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