Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

Gamma-Interferon-Inducible Lysosomal Thiol Reductase (GILT)

  • Lydia R. Meador
  • Karen Taraszka HastingsEmail author
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_101662


Historical Background

In 1988, the laboratory of Dr. Jeffrey Ravetch characterized a gene which is upregulated upon exposure to the cytokine, interferon-γ (IFN-γ). The protein is produced in a precursor form of 35 kDa and processed into a mature form of 30 kDa. The protein was originally named inducible protein 30 (IP30) and the gene named IFI30. IP30 is constitutively expressed in many antigen-presenting cells (APCs) and induced in other cell types including fibroblasts, endothelial cells, and keratinocytes (Maric et al. 2001; Lackman and Cresswell 2006; Phipps-Yonas et al. 2013a; Nguyen et al. 2016).

Homology to protein folding patterns of a cellular thiol reductase, thioredoxin, suggested that IP30 may be capable of breaking disulfide bonds. Indeed, a thioredoxin-like motif, CXXC, is found in the IP30 protein sequence and is conserved across species with IP30 homologs. IP30 reduces disulfide bonds, and the cysteines in the CXXC...

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© Springer International Publishing AG 2018

Authors and Affiliations

  1. 1.Department of Basic Medical Sciences, College of MedicineUniversity of ArizonaPhoenixUSA