Cited by 126Redox biology and oxidative stressCytokine Signaling Pathways and InteractionsSulfur Compounds in Biology

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S-Glutathionylation Impairs Signal Transducer and Activator of Transcription 3 Activation and Signaling

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Xie, Yi, Kole, Sutapa, Precht, Patricia, Pazin, Michael J., Bernier, Michel·2009·Endocrinology

DOI 10.1210/en.2008-1241PMC PMC2654735

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Abstract

S-glutathionylation is a physiological, reversible protein modification of cysteine residues with glutathione in response to mild oxidative stress. Because the key cell growth regulator signal transducer and activator of transcription (STAT) 3 is particularly susceptible to redox regulation, we hypothesized that oxidative modification of cysteine residues of STAT3 by S-glutathionylation may occur. Herein, we show that the cysteine residues of STAT3 are modified by a thiol-alkylating agent and are the targets of S-glutathionylation. STAT3 protein thiol reactivity was reversibly attenuated with concomitant increase in the S-glutathionylation of STAT3 upon treatment of human HepG2 hepatoma cells with pyrrolidine dithiocarbamate, glutathione disulfide, or diamide. Under these conditions there was a marked reduction in IL-6-dependent STAT3 signaling, including decreased STAT3 tyrosine phosphorylation, loss in nuclear accumulation of STAT3, and impaired expression of target genes, such as fibrinogen-γ. In a cell-free system, diamide induced glutathionylation of STAT3, which was decreased upon addition of glutaredoxin (GRX)-1, a deglutathionylation enzyme, or the reducing agent, dithiothreitol. Glutathionylated STAT3 was a poor Janus protein tyrosine kinase 2 substrate in vitro, and it exhibited low DNA-binding activity. Cellular GRX-1 activity was inhibited by diamide and pyrrolidine dithiocarbamate treatment; however, ectopic expression of GRX-1 was accompanied by a modest increase in phosphorylation, nuclear translocation, and DNA-binding ability of STAT3 in response to IL-6. These results are the first to show S-glutathionylation of STAT3, a modification that may exert regulatory function in STAT3 signaling. Reversible S-glutathionylation of STAT3 regulates its activity as transcription factor.

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Authors: Xie, Y., Kole, S., Precht, P., Pazin, M. J., & Bernier, M.
Affiliations: National Institutes of Health (US)
MedStar Health Research Institute (US)
Corresponding author: Bernier, Michel
ORCID: Xie, Yi
Pazin, Michael J.
Bernier, Michel
Venue: Endocrinology
Publisher: The Endocrine Society
Published: 2008-11-06
Volume: 150
Issue: 3
Pages: 1122-1131
ISSN: 0013-7227 (ISSN-L)
1945-7170
DOI: 10.1210/en.2008-1241
PMC: PMC2654735
OpenAlex: W1996740511
Cited by: 126
References: 61
Citations by year: 2026: 3 · 2025: 3 · 2024: 4 · 2023: 4 · 2022: 4 · 2021: 9 · 2020: 10 · 2019: 8 · 2018: 4 · 2017: 11 · 2016: 7 · 2015: 9 · 2014: 13 · 2013: 12 · 2012: 5
FWCI: 2.75
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Endocrinology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute on Aging (ZIAAG000378)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
Keywords: S-glutathionylation, STAT3, cysteine oxidation, glutaredoxin 1, IL-6 signaling, STAT3 tyrosine phosphorylation, nuclear translocation, DNA-binding activity, oxidative stress, diamide, pyrrolidine dithiocarbamate, protein thiol modification
MeSH terms: Antioxidants, Cells, Cultured, Cysteine, Diamines, Glutathione, Humans, Phosphorylation, Protein Processing, Post-Translational, Pyrrolidines, Thiocarbamates, Transfection, Signal Transduction, Interleukin-6, Oxidants, STAT3 Transcription Factor, Janus Kinase 2, Glutaredoxins

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S-Glutathionylation Impairs Signal Transducer and Activator of Transcription 3 Activation and Signaling

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