Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF‐κB

Chen, Lin‐feng; Mu, Yajun; Greene, Warner C.

doi:10.1093/emboj/cdf660

Cited by 827NF-κB Signaling PathwaysGenomics and Chromatin DynamicsSignaling Pathways in Disease

Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF‐κB

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Chen, Lin‐feng, Mu, Yajun, Greene, Warner C.·2002·The EMBO Journal

DOI 10.1093/emboj/cdf660PMC PMC136963

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Abstract

The nuclear function of the heterodimeric NF-kappaB transcription factor is regulated in part through reversible acetylation of its RelA subunit. We now demonstrate that the p300 and CBP acetyltransferases play a major role in the in vivo acetylation of RelA, principally targeting lysines 218, 221 and 310 for modification. Analysis of the functional properties of hypoacetylated RelA mutants containing lysine-to-arginine substitutions at these sites and of wild-type RelA co-expressed in the presence of a dominantly interfering mutant of p300 reveals that acetylation at lysine 221 in RelA enhances DNA binding and impairs assembly with IkappaBalpha. Conversely, acetylation of lysine 310 is required for full transcriptional activity of RelA in the absence of effects on DNA binding and IkappaBalpha assembly. Together, these findings highlight how site-specific acetylation of RelA differentially regulates distinct biological activities of the NF-kappaB transcription factor complex.

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p300 and CREB binding protein acetylate p65 at Lys218, 221, and 310, which boosts p65 DNA binding and blocks its binding to nuclear IκBα, thereby regulating transcription.
“It is our particular interest that acetylation of p65 at Lys218, 221 and 310 by p300 and cAMP response element binding (CREB) binding protein (CBP) regulates its transcriptional activity by increasing p65 DNA binding and by inhibiting its association with nuclear IκBα for the prevention of NF-κB relocation to the cytoplasm [55].”
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 [55]

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Authors: Chen, L., Mu, Y., & Greene, W. C.
Affiliations: University of California, San Francisco (US)
Corresponding author: Greene, Warner C.
ORCID: Greene, Warner C.
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2002-12-01
Volume: 21
Issue: 23
Pages: 6539-6548
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1093/emboj/cdf660
PMC: PMC136963
OpenAlex: W2004335766
Cited by: 827
References: 56
Citations by year: 2026: 18 · 2025: 37 · 2024: 34 · 2023: 33 · 2022: 26 · 2021: 54 · 2020: 24 · 2019: 31 · 2018: 22 · 2017: 33 · 2016: 41 · 2015: 25 · 2014: 41 · 2013: 63 · 2012: 48
FWCI: 9.55
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Yale University
Gladstone Institutes
National Institutes of Health
University of Illinois at Urbana-Champaign
Center for AIDS Research, University of Washington
University of California, San Francisco
National Institute of Mental Health (P30MH059037, P30-MH 59037)
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: NF-κB, RelA, acetylation, P300, CBP, lysine acetylation sites, IκBα, DNA binding, transcriptional activity, post-translational modification, transcription factor regulation
MeSH terms: p300-CBP-Associated Factor, Acetylation, Acetyltransferases, Cell Nucleus, Enhancer Elements, Genetic, Mutation, Transcription Factors, NF-kappa B, Cell Cycle Proteins, p300-CBP Transcription Factors, Histone Acetyltransferases, Transcription Factor RelA

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Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF‐κB

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