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Receptor-interacting Protein 140 Directly Recruits Histone Deacetylases for Gene Silencing
Open accessAbstract
Receptor-interacting protein 140 (RIP140) encodes a histone deacetylase (HDAC) inhibitor-sensitive repressive activity. Direct interaction of RIP140 with HDAC1 and HDAC3 occurs in vitro and in vivo as demonstrated in co-immunoprecipitation and glutathione S-transferase pull-down experiments. The HDAC-interacting domain of RIP140 is mapped to its N-terminal domain, between amino acids 78 and 303 based upon glutathione S-transferase pull-down experiments. In chromatin immunoprecipitation assays, it is demonstrated that histone deacetylation occurs at the chromatin region of the Gal4 binding sites as a result of Gal4 DNA binding domain-tethered RIP expression. The immunocomplexes of RIP140 from cells transfected with RIP140 and HDAC are able to deacetylate histone proteins in vitro. This study presents the first evidence for RIP140 as a negative coregulator for nuclear receptor actions by directly recruiting histone deacetylases and categorizes RIP140 as a novel negative coregulator that is able to directly interact with HDACs.
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“At the end of the transcriptional response, liganded RARs have been shown to recruit unconventional coregulators with LxxLL motifs, such as RIP140 and PRAME ( Fig. 4C ).”
From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [108]
In the citing paper
“In contrast to the classical p160 coregulators, RIP140 and PRAME inhibit the transcriptional activity of RARs through the recruitment of HDACs ( 108 ) and PcG proteins ( 63 ) respectively.”
From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [108]
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Metadata
- Authors
- Wei, L.-N., Hu, X., Chandra, D., Seto, E., & Farooqui, M.
- Affiliations
- University of Minnesota (US)
- University of South Florida (US)
- Corresponding author
- Wei, Li-Na
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-12
- Volume
- 275
- Issue
- 52
- Pages
- 40782-40787
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1969973975
- Cited by
- 150
- References
- 42
- Citations by year
- 2026: 1 · 2025: 1 · 2023: 1 · 2022: 3 · 2019: 1 · 2018: 3 · 2017: 5 · 2016: 2 · 2015: 6 · 2014: 6 · 2013: 3 · 2012: 5
- FWCI
- 3.14
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases ([DK54733, R01DK054733)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- RIP140, histone deacetylase, HDAC1, HDAC3, gene silencing, histone deacetylation, protein-protein interaction, chromatin
- MeSH terms
- Nuclear Receptor Interacting Protein 1, Animals, Binding Sites, Chromatin, Histone Deacetylases, Histones, Hydroxamic Acids, Nuclear Proteins, Tretinoin, Receptors, Tumor Necrosis Factor, COS Cells, Gene Silencing, Adaptor Proteins, Signal Transducing, Receptors, TNF-Related Apoptosis-Inducing Ligand
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