Cited by 150Histone Deacetylase Inhibitors ResearchGenomics and Chromatin DynamicsEpigenetics and DNA Methylation

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Receptor-interacting Protein 140 Directly Recruits Histone Deacetylases for Gene Silencing

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Wei, Li-Na, Hu, Xinli, Chandra, Dhyan, Seto, Edward, Farooqui, Maria·2000·Journal of Biological Chemistry

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Abstract

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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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
ORCID: Wei, Li-Na
Hu, Xinli
Chandra, Dhyan
Seto, Edward
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2000-12
Volume: 275
Issue: 52
Pages: 40782-40787
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m004821200
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7248 d)
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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Receptor-interacting Protein 140 Directly Recruits Histone Deacetylases for Gene Silencing

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