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Immunoproteasome-specific inhibitors and their application

Michael Basler1, Marcus Groettrup

  • 1Department of Biology, Division of Immunology, University of Konstanz, Konstanz, Germany. michael.basler@uni-konstanz.de

Methods in Molecular Biology (Clifton, N.J.)
|February 22, 2012
PubMed

Immunoproteasomes (IPs) containing the interferon-inducible subunits β1i (LMP2), β2i (MECL-1), and β5i (LMP7) alter proteasomal cleavage preference, optimise the generation of peptide ligands of MHC class I molecules, alter cytokine profile, influence T-helper cell differentiation, and play a role in T-cell survival. Small molecule inhibitors are useful tools for probing the role of the immunoproteasome in immune functions. Here, we describe different methods to characterise immunoproteasome-selective inhibitors. Thereby, we provide the methodology to analyse the specificity and cell permeability of immunoproteasome inhibitors, as well as to functionally investigate immunoproteasome inhibitors in antigen presentation.

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