Cited by 438NF-κB Signaling PathwaysGenomics and Chromatin DynamicsSignaling Pathways in Disease

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NF-κB RelA Phosphorylation Regulates RelA Acetylation

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Chen, Lin-Feng, Williams, Samuel A., Mu, Yajun, Nakano, Hiroyasu, Duerr, James M., Buckbinder, Leonard, Greene, Warner C.·2005·Molecular and Cellular Biology

DOI 10.1128/mcb.25.18.7966-7975.2005PMC PMC1234328

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Abstract

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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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.
ORCID: Chen, Lin-Feng
Williams, Samuel A.
Nakano, Hiroyasu
Buckbinder, Leonard
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
DOI: 10.1128/mcb.25.18.7966-7975.2005
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
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
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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NF-κB RelA Phosphorylation Regulates RelA Acetylation

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