ArticleProceedings of the National Academy of Sciences of the United States of America2002
Role of the C-terminal propeptide in the activity and maturation of gamma -interferon-inducible lysosomal thiol reductase (GILT).
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 31 citations in OpenAlex.
- GILT stabilizes cofilin to promote the metastasis of prostate cancer.Cell death discovery · 2025Article
- Low-dose cadmium potentiates lung inflammatory response to 2009 pandemic H1N1 influenza virus in mice.Environment international · 2019Article
- AS-48 bacteriocin: close to perfection.Cellular and molecular life sciences : CMLS · 2011Review
- Disulfide reduction in the endocytic pathway: immunological functions of gamma-interferon-inducible lysosomal thiol reductase.Antioxidants & redox signaling · 2011Review
- Insights into the functionality of the putative residues involved in enterocin AS-48 maturation.Applied and environmental microbiology · 2010Article
- The transcriptome of the fetal inflammatory response syndrome.American journal of reproductive immunology (New York, N.Y. : 1989) · 2010Article
- Article
- Gene expression profiling of Japanese psoriatic skin reveals an increased activity in molecular stress and immune response signals.Journal of molecular medicine (Berlin, Germany) · 2005Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
gamma-Interferon-inducible lysosomal thiol reductase (GILT) is constitutively expressed in antigen-presenting cells. GILT facilitates unfolding of endocytosed antigens in MHC class II-containing compartments by enzymatically reducing disulfide bonds. The enzyme is synthesized as a 35-kDa precursor. Although a fraction of the precursor is secreted as a disulfide-linked dimer, the majority is directed via the mannose-6-phosphate receptor pathway to endocytic compartments where its N- and C-terminal propeptides are cleaved to generate the 30-kDa mature form. Both precursor and mature GILT reduce disulfide bonds with an acidic pH optimum. In this report, we show that the cysteine residues in the C-terminal propeptide, Cys-211 and Cys-222, serve key structural roles. Mutation of Cys-222 abolishes disulfide-linked dimerization of precursor GILT and decreases the efficiency of GILT maturation. Mutation of Cys-211 results in both impaired intracellular maturation and loss of enzymatic activity of the precursor form at an acidic pH. A similar phenotype was obtained upon mutation of Cys-200, which is retained in the mature form. Cys-200 and Cys-211 seem to form a disulfide bond that links the propeptide and the mature enzyme until reduction in the lysosome. This disulfide bridge is essential for stability of the enzyme at low pH and for its proper maturation in vivo.
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Registered trials
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