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NF-κB RelA Phosphorylation Regulates RelA Acetylation
Open accessAbstract
The nuclear functions of NF-kappaB p50/RelA heterodimers are regulated in part by posttranslational modifications of its RelA subunit, including phosphorylation and acetylation. Acetylation at lysines 218, 221, and 310 differentially regulates RelA's DNA binding activity, assembly with IkappaBalpha, and transcriptional activity. However, it remains unclear whether the acetylation is regulated or simply due to stimulus-coupled nuclear translocation of NF-kappaB. Using anti-acetylated lysine 310 RelA antibodies, we detected p300-mediated acetylation of RelA in vitro and in vivo after stimulation of cells with tumor necrosis factor alpha (TNF-alpha). Coexpression of catalytically inactive mutants of the catalytic subunit of protein kinase A/mitogen- and stress-activated kinase 1 or IKK1/IKK2, which phosphorylate RelA on serine 276 or serine 536, respectively, sharply inhibited RelA acetylation on lysine 310. Furthermore, phosphorylation of RelA on serine 276 or serine 536 increased assembly of phospho-RelA with p300, which enhanced acetylation on lysine 310. Reconstitution of RelA-deficient murine embryonic fibroblasts with RelA S276A or RelA S536A decreased TNF-alpha-induced acetylation of lysine 310 and expression of the endogenous NF-kappaB-responsive E-selectin gene. These findings indicate that the acetylation of RelA at lysine 310 is importantly regulated by prior phosphorylation of serines 276 and 536. Such phosphorylated and acetylated forms of RelA display enhanced transcriptional activity.
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“Extracellular inflammatory signals including lipopolysaccharide (LPS), pro-inflammatory cytokines, reactive oxygen species, advanced glycation end products, and oxidized low-density lipoprotein trigger the phosphorylation of IKKβ, which in turn phosphorylates IκBα for ubiquitination and degradation by proteasome [13–18].”
From Edible blue-green algae reduce the production of pro-inflammatory cytokines by inhibiting NF-κB pathway in macrophages and splenocytes (2013) · cites this paper as [13]
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Exploring the Role of EBP50 in Vascular Inflammation
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Metadata
- Authors
- Chen, L.-F., Williams, S. A., Mu, Y., Nakano, H., Duerr, J. M., Buckbinder, L., & Greene, W. C.
- Affiliations
- Gladstone Institutes (US)
- Juntendo University (JP)
- Pfizer (United States) (US)
- Corresponding author
- Chen, Lin-Feng
- Greene, Warner C.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2005-09-01
- Volume
- 25
- Issue
- 18
- Pages
- 7966-7975
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC1234328
- OpenAlex
- W2117817795
- Cited by
- 438
- References
- 36
- Citations by year
- 2026: 10 · 2025: 8 · 2024: 13 · 2023: 12 · 2022: 11 · 2021: 24 · 2020: 25 · 2019: 14 · 2018: 24 · 2017: 22 · 2016: 19 · 2015: 15 · 2014: 25 · 2013: 29 · 2012: 34
- FWCI
- 7.32
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Foundation for the National Institutes of Health
- Arthritis Foundation
- Pfizer
- Gladstone Institutes
- Center for AIDS Research, University of Washington
- University of California, San Francisco
- National Institute of Mental Health (P30MH059037, P30-MH 59037)
- National Cancer Institute (R01CA089001, R01 CA89001-02)
- National Institute of Allergy and Infectious Diseases (AI07305)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- p65 phosphorylation, P300, protein kinase A, TNF-α, E-selectin, transcriptional activity, post-translational modification, embryonic fibroblasts
- MeSH terms
- Acetylation, Animals, Cells, Cultured, Humans, Lysine, Mutation, Nuclear Proteins, Phosphorylation, Serine, Transcription, Genetic, Trans-Activators, NF-kappa B, E1A-Associated p300 Protein, Mice, Transcription Factor RelA
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