Immunoproteasomes: Structure, function, and antigen presentation

Deborah A. Ferrington, Dale S. Gregerson

Research output: Chapter in Book/Report/Conference proceedingChapter

268 Scopus citations


Immunoproteasomes contain replacements for the three catalytic subunits of standard proteasomes. In most cells, oxidative stress and proinflammatory cytokines are stimuli that lead to elevated production of immunoproteasomes. Immune system cells, especially antigen-presenting cells, express a higher basal level of immunoproteasomes. A well-described function of immunoproteasomes is to generate peptides with a hydrophobic C terminus that can be processed to fit in the groove of MHC class I molecules. This display of peptides on the cell surface allows surveillance by CD8 T cells of the adaptive immune system for pathogen-infected cells. Functions of immunoproteasomes, other than generating peptides for antigen presentation, are emerging from studies in immunoproteasome-deficient mice, and are complemented by recently described diseases linked to mutations or single-nucleotide polymorphisms in immunoproteasome subunits. Thus, this growing body of literature suggests a more pleiotropic role in cell function for the immunoproteasome.

Original languageEnglish (US)
Title of host publicationProgress in Molecular Biology and Translational Science
PublisherElsevier B.V.
Number of pages38
StatePublished - 2012

Publication series

NameProgress in Molecular Biology and Translational Science
ISSN (Print)1877-1173


  • Antigen presentation
  • Immunoproteasome
  • Knockout mice
  • LMP2
  • LMP7
  • MECL-1
  • MHC class I
  • Oxidation
  • PSMB8-associated disease


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