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Enzymatic Activity Associated with Class II HDACs Is Dependent on a Multiprotein Complex Containing HDAC3 and SMRT/N-CoR
Open accessAbstract
Histone deacetylases (HDACs) play a key role in regulating eukaryotic gene expression. The HDAC domain, homologous to the yeast repressors RPD3 and HDA1, is considered necessary and sufficient for enzymatic activity. Here, we show that the catalytic domain of HDAC4 interacts with HDAC3 via the transcriptional corepressor N-CoR/SMRT. All experimental conditions leading to the suppression of HDAC4 binding to SMRT/N-CoR and to HDAC3 result in the loss of enzymatic activity associated with HDAC4. In vitro reconstitution experiments indicate that HDAC4 and other class II HDACs are inactive in the context of the SMRT/N-CoR-HDAC3 complex and do not contribute to its enzymatic activity. These observations indicate that class II HDACs regulate transcription by bridging the enzymatically active SMRT/N-CoR-HDAC3 complex and select transcription factors independently of any intrinsic HDAC activity.
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“In particular, HDAC4 and -7 were shown to associate with HDAC3-SMRT/N-CoR complexes through their HDAC domains (19,20).”
From Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases (2007) · cites this paper as [20]
In the citing paper
“Site-directed mutagenesis of conserved active site residues in HDAC4 failed to clarify this point in that all HDAC4 mutants showing impaired deacetylase activity in vitro also lost the ability to interact with HDAC3-SMRT/N-CoR complexes (20).”
From Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases (2007) · cites this paper as [20]
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Metadata
- Authors
- Fischle, W., Dequiedt, F., Hendzel, M. J., Guenther, M. G., Lazar, M. A., Voelter, W., & Verdin, E.
- Affiliations
- University of California, San Francisco (US)
- University of Alberta (CA)
- University of Pennsylvania (US)
- University of Tübingen (DE)
- Corresponding author
- Verdin, Eric
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2002-01
- Volume
- 9
- Issue
- 1
- Pages
- 45-57
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2052373759
- Cited by
- 754
- References
- 60
- Citations by year
- 2026: 16 · 2025: 20 · 2024: 26 · 2023: 12 · 2022: 32 · 2021: 23 · 2020: 31 · 2019: 39 · 2018: 29 · 2017: 34 · 2016: 33 · 2015: 43 · 2014: 42 · 2013: 46 · 2012: 41
- FWCI
- 9.99
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 4215 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Open Repository and Bibliography (University of Liège) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM051671, GM51671)
- 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
- histone deacetylase, class II HDACs, HDAC4, HDAC3, SMRT, NCoR, corepressors, protein complexes, transcriptional repression, gene expression regulation, repressors
- MeSH terms
- Histone Deacetylase 3, Amino Acid Sequence, DNA Mutational Analysis, DNA-Binding Proteins, Enzyme Activation, HeLa Cells, Histone Deacetylases, Humans, Molecular Sequence Data, Protein Binding, Repressor Proteins, Transcription, Genetic, Nuclear Receptor Co-Repressor 2
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