The histone deacetylase-3 complex contains nuclear receptor corepressors
Open accessAbstract
Acetylation and deacetylation of nucleosomal histones have profound effects on gene transcription in all eukaryotes. In humans, three highly homologous class I and four class II histone deacetylase (HDAC) enzymes have been identified to date. The class I deacetylases HDAC1 and HDAC2 are components of multisubunit complexes, one of which could associate with the nuclear hormone receptor corepressor, N-CoR. N-CoR also interacts with class II deacetylases HDAC4, HDAC5, and HDAC7. In comparison with HDAC1 and HDAC2, HDAC3 remains relatively uncharacterized, and very few proteins have been shown to interact with HDAC3. Using an affinity purification approach, we isolated an enzymatically active HDAC3 complex that contained members of the nuclear receptor corepressor family. Deletion analysis of N-CoR revealed that HDAC3 binds multiple N-CoR regions in vitro and that all of these regions are required for maximal binding in vivo . The N-CoR domains that interact with HDAC3 are distinct from those that bind other HDACs. Transient overexpression of HDAC3 and microinjection of Abs against HDAC3 showed that a component of transcriptional repression mediated by N-CoR depends on HDAC3. Interestingly, data suggest that interaction with a region of N-CoR augments the deacetylase activity of HDAC3. These results provide a possible molecular mechanism for HDAC3 regulation and argue that N-CoR is a platform in which distinct domains can interact with most of the known HDACs.
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HDAC3 appears to be uniquely recruited to the SMRT/NCoR complex, where it interacts with a conserved deacetylase-activation-domain (DAD) within SMRT or NCoR.
“In contrast, HDAC3 appears to be uniquely recruited to the SMRT/NCoR complex where it interacts with a conserved deacetylase-activation-domain (DAD) within SMRT or NCoR8,10,12,24,25,26.”
From Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate (2012) · cites this paper as [12]
The Discussion (page not available in our copy) describes an HDAC3–N-CoR/SMRT complex, and the Results show that HDAC3 binds N-CoR regions distinct from those used by other HDACs. The paper does not identify a conserved deacetylase-activation domain (DAD) in SMRT or N-CoR as the binding site; it instead reports binding to multiple N-CoR regions. (LLM, conf=0.88)
Experimental — accuracy not yet measuredHDACs 1, 2 and 3 require association with large multisubunit corepressor complexes for maximal activity.
“HDACs 1, 2 and 3 require association with large multisubunit corepressor complexes for maximal activity7-12.”
From Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate (2012) · cites this paper as [12]
The introduction describes HDAC1 and HDAC2 as components of multisubunit complexes, and the Results identify an enzymatically active HDAC3 complex. The Results also show that an N-CoR fragment increases HDAC3 activity, but do not establish that association with a large complex is required for maximal activity of all three enzymes; the same experiment found no enhancement of HDAC1 activity by that fragment. Page numbers were not available in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThe DAD both recruits and activates HDAC3.
“The DAD both recruits and activates HDAC310-12.”
From Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate (2012) · cites this paper as [12]
Recent studies indicate that the corepressors N-CoR and SMRT are preferentially assembled into the HDAC3 complex, but not into the HDAC1 or HDAC2 complex, suggesting that HDAC3 has a functional activity distinct from those of other class I histone deacetylases.
“recent studies indicate that the corepressors N-CoR and SMRT are preferentially assembled into the HDAC3 complex, but not into the HDAC1 or HDAC2 complex, suggesting that HDAC3 has a functional activity distinct from those of other class I histone deacetylases (27, 58).”
From Gamma Interferon Triggers Interaction between ICSBP (IRF-8) and TEL, Recruiting the Histone Deacetylase HDAC3 to the Interferon-Responsive Element (2002) · cites this paper as [58]
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- Authors
- Wen, Y.-D., Perissi, V., Staszewski, L. M., Yang, W.-M., Krones, A., Glass, C. K., Rosenfeld, M. G., & Seto, E.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Seto, Edward
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2000-06-20
- Volume
- 97
- Issue
- 13
- Pages
- 7202-7207
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC16523
- OpenAlex
- W2092349389
- Cited by
- 378
- References
- 30
- Citations by year
- 2026: 6 · 2025: 6 · 2024: 14 · 2023: 11 · 2022: 5 · 2021: 6 · 2020: 19 · 2019: 15 · 2018: 7 · 2017: 5 · 2016: 12 · 2015: 17 · 2014: 15 · 2013: 17 · 2012: 15
- FWCI
- 9.99
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01es009262-05)
- National Institute of General Medical Sciences (R01GM058486, GM58486)
- National Institute of Environmental Health Sciences (ES09262)
- 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
- HDAC3, nuclear receptor corepressor, NCoR, histone deacetylase complex, transcriptional repression, protein-protein interaction, HDAC1, HDAC2, HDAC4, HDAC5, HDAC7
- MeSH terms
- Acetylation, Amino Acid Sequence, HeLa Cells, Histone Deacetylases, Humans, Molecular Sequence Data, Signal Transduction, Receptors, Cytoplasmic and Nuclear
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