The immunoproteasome in antigen processing and other immunological functions

Curr Opin Immunol. 2013 Feb;25(1):74-80. doi: 10.1016/j.coi.2012.11.004. Epub 2012 Dec 6.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Antigen Presentation / genetics
  • Autoimmune Diseases / drug therapy
  • Autoimmune Diseases / genetics
  • Autoimmune Diseases / immunology*
  • Crystallography, X-Ray
  • Humans
  • Mice
  • Mice, Knockout
  • Molecular Conformation
  • Multiprotein Complexes / chemistry
  • Multiprotein Complexes / immunology*
  • Proteasome Endopeptidase Complex / genetics
  • Proteasome Endopeptidase Complex / immunology*
  • Proteasome Endopeptidase Complex / metabolism
  • Proteasome Inhibitors / therapeutic use
  • Structure-Activity Relationship
  • T-Lymphocytes, Helper-Inducer / immunology*


  • Multiprotein Complexes
  • Proteasome Inhibitors
  • LMP7 protein
  • Proteasome Endopeptidase Complex