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Dynamic redox control of NF-κB through glutaredoxin-regulated S-glutathionylation of inhibitory κB kinase β
Open accessAbstract
The transcription factor NF-κB, a central regulator of immunity, is subject to regulation by redox changes. We now report that cysteine-179 of the inhibitory κB kinase (IKK) β-subunit of the IKK signalosome is a central target for oxidative inactivation by means of S-glutathionylation. S-glutathionylation of IKK-β Cys-179 is reversed by glutaredoxin (GRX), which restores kinase activity. Conversely, GRX1 knockdown sensitizes cells to oxidative inactivation of IKK-β and dampens TNF-α-induced IKK and NF-κB activation. Primary tracheal epithelial cells from Glrx1 -deficient mice display reduced NF-κB DNA binding, RelA nuclear translocation, and MIP-2 (macrophage inflammatory protein 2) and keratinocyte-derived chemokine production in response to LPS. Collectively, these findings demonstrate the physiological relevance of the S-glutathionylation–GRX redox module in controlling the magnitude of activation of the NF-κB pathway.
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“In addition, I-κB-Kinase (IKK) complex is the core component of NF-κB and is a target of ROS, affecting thus NF-κB and S-glutathionylation and inhibited IKKβ activity (Reynaert et al. 2006).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Reynaert et al. 2006
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Cites
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125
A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
DiDonato, J. A., Hayakawa, M., Rothwarf, D. M., Zandi, E., & Karin, M. (1997) · Nature · doi:10.1038/41493 · Cited by 2,125
IKK-1 and IKK-2: Cytokine-Activated IκB Kinases Essential for NF-κB Activation
Mercurio, F., Zhu, H., Murray, B. W., Shevchenko, A., Bennett, B. L., Li, J. W., Young, D. B., Barbosa, M. S., Mann, M., Manning, A. M., et al. (1997) · Science · doi:10.1126/science.278.5339.860 · Cited by 2,042
Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IκB kinase
Rossi, A., Kapahi, P., Natoli, G., Takahashi, T., Chen, Y., Karin, M., & Santoro, M. G. (2000) · Nature · doi:10.1038/47520 · Cited by 1,303
IKK-γ is an essential regulatory subunit of the IκB kinase complex
Rothwarf, D. M., Zandi, E., Natoli, G., & Karin, M. (1998) · Nature · doi:10.1038/26261 · Cited by 958
Positive and Negative Regulation of IκB Kinase Activity Through IKKβ Subunit Phosphorylation
Delhase, M., Hayakawa, M., Chen, Y., & Karin, M. (1999) · Science · doi:10.1126/science.284.5412.309 · Cited by 852
Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD
Budanov, A. V., Sablina, A. A., Feinstein, E., Koonin, E. V., & Chumakov, P. M. (2004) · Science · doi:10.1126/science.1095569 · Cited by 731
Fernandes, A. P., & Holmgren, A. (2004) · Antioxidants and Redox Signaling · doi:10.1089/152308604771978354 · Cited by 670
S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
Adachi, T. K., Weisbrod, R. M., Pimentel, D. R., Ying, J., Sharov, V. S., Schöneich, C., & Cohen, R. A. (2004) · Nature Medicine · doi:10.1038/nm1119 · Cited by 662
Histone H3 phosphorylation by IKK-α is critical for cytokine-induced gene expression
Yamamoto, Y., Verma, U. N., Prajapati, S., Kwak, Y.-T., & Gaynor, R. B. (2003) · Nature · doi:10.1038/nature01576 · Cited by 577
Research works printed but not linked: 1
- Y. M. Janssen, K. E. Driscoll, B. Howard, T. R. Quinlan, M. Treadwell, A. Barchowsky, B. T. Mossman Am. J. Pathol. 151, 389–401 (1997).
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Marzano, V., Santini, S., Rossi, C., Zucchelli, M., D’Alessandro, A., Marchetti, C., Mingardi, M., Stagni, V., Barilà, D., & Urbani, A. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.05.029 · Cited by 23
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Metadata
- Authors
- Reynaert, N. L., van der Vliet, A., Guala, A. S., McGovern, T., Hristova, M., Pantano, C., Heintz, N. H., Heim, J., Ho, Y.-S., Matthews, D. E., Wouters, E. F. M., & Janssen-Heininger, Y. M. W.
- Affiliations
- Maastricht University (NL)
- Departments of *Pathology and
- University of Vermont (US)
- Wayne State University (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2006-08-29
- Volume
- 103
- Issue
- 35
- Pages
- 13086-13091
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1559757
- OpenAlex
- W2166902551
- Cited by
- 442
- References
- 37
- Citations by year
- 2026: 19 · 2025: 12 · 2024: 19 · 2023: 19 · 2022: 18 · 2021: 20 · 2020: 23 · 2019: 23 · 2018: 13 · 2017: 25 · 2016: 18 · 2015: 24 · 2014: 22 · 2013: 28 · 2012: 29
- FWCI
- 9.51
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Research Publications (Maastricht University) (submittedVersion, other-oa)
- Funders
- National Institutes of Health (P20 RL15557)
- U.S. Public Health Service (P20 RL-15557)
- National Heart, Lung, and Blood Institute (R01 HL60014, P01 HL074295, R01HL074295, R01HL060812, R01HL060014, HL 60812)
- National Center for Research Resources (P20RR015557)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Keywords
- NF-κB, S-glutathionylation, glutaredoxin, redox regulation, oxidative inactivation, TNF signaling, tracheal epithelial cells, lipopolysaccharide response, chemokine production, p65 nuclear translocation
- MeSH terms
- Animals, Cells, Cultured, Cysteine, Glutathione, Hydrogen Peroxide, Lipopolysaccharides, Mice, Inbred C57BL, Oxidation-Reduction, Oxidoreductases, Respiratory System, Sulfenic Acids, Keratinocytes, Monokines, NF-kappa B, Chemokines, Protein Subunits, Mice, I-kappa B Kinase, Chemokine CXCL2, Glutaredoxins
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