The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Brd4 Coactivates Transcriptional Activation of NF-κB via Specific Binding to Acetylated RelA
Open accessAbstract
Acetylation of the RelA subunit of NF-kappaB, especially at lysine-310, is critical for the transcriptional activation of NF-kappaB and the expression of inflammatory genes. In this study, we demonstrate that bromodomains of Brd4 bind to acetylated lysine-310. Brd4 enhances transcriptional activation of NF-kappaB and the expression of a subset of NF-kappaB-responsive inflammatory genes in an acetylated lysine-310-dependent manner. Bromodomains of Brd4 and acetylated lysine-310 of RelA are both required for the mutual interaction and coactivation function of Brd4. Finally, we demonstrate that Brd4 further recruits CDK9 to phosphorylate C-terminal domain of RNA polymerase II and facilitate the transcription of NF-kappaB-dependent inflammatory genes. Our results identify Brd4 as a novel coactivator of NF-kappaB through specifically binding to acetylated lysine-310 of RelA. In addition, these studies reveal a mechanism by which acetylated RelA stimulates the transcriptional activity of NF-kappaB and the NF-kappaB-dependent inflammatory response.
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Self-citationDuration of Nuclear NF-κB Action Regulated by Reversible Acetylation
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Metadata
- Authors
- Huang, B., Yang, X.-D., Zhou, M.-M., Ozato, K., & Chen, L.-F.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2009-03-01
- Volume
- 29
- Issue
- 5
- Pages
- 1375-1387
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2017789254
- Cited by
- 579
- References
- 51
- FWCI
- 3.64
- Type
- journal article
- Language
- en
- Open access
- green
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- Huang, B., Yang, X.-D., Zhou, M.-M., Ozato, K., & Chen, L.-F. (2009). Brd4 Coactivates Transcriptional Activation of NF-κB via Specific Binding to Acetylated RelA. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.01365-08
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