Diverse cellular and organismal functions of the lysosomal thiol reductase GILT

Matthew P. Rausch, Karen Taraszka Hastings

Research output: Contribution to journalReview articlepeer-review

29 Scopus citations


Gamma-interferon-inducible lysosomal thiol reductase (GILT) is the only enzyme known to catalyze disulfide bond reduction in the endocytic pathway. GILT facilitates the presentation of a subset of epitopes from disulfide bond-containing antigens. Enhanced presentation of MHC class II-restricted epitopes alters central tolerance and modulates CD4+ T cell-mediated autoimmunity. Improved cross-presentation of viral epitopes results in improved cross-priming of viral-specific CD8+ T cells. GILT regulates the cellular redox state. In GILT-/- cells, there is a shift from the reduced to the oxidized form of glutathione, resulting in mitochondrial autophagy, decreased superoxide dismutase 2, and elevated superoxide levels. GILT expression diminishes cellular activation, including decreased phosphorylated ERK1/2, and decreases cellular proliferation. GILT enhances the activity of bacterial hemolysins, such as listeriolysin O, and increases bacterial replication and infection. GILT expression in cancer cells is associated with improved patient survival. These diverse roles of GILT are discussed.

Original languageEnglish (US)
Pages (from-to)124-128
Number of pages5
JournalMolecular Immunology
Issue number2
StatePublished - Apr 16 2015


  • Antigen presentation
  • Autoimmunity
  • Cancer
  • GILT
  • IFI30
  • Redox

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology


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