Cited by 762Histone Deacetylase Inhibitors ResearchGenomics and Chromatin DynamicsEpigenetics and DNA Methylation

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Enzymatic Activity Associated with Class II HDACs Is Dependent on a Multiprotein Complex Containing HDAC3 and SMRT/N-CoR

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Fischle, Wolfgang, Dequiedt, Franck, Hendzel, Michael J, Guenther, Matthew G, Lazar, Mitchell A, Voelter, Wolfgang, Verdin, Eric·2002·Molecular Cell

DOI 10.1016/s1097-2765(01)00429-4

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Abstract

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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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: Fischle, Wolfgang
Hendzel, Michael J
Guenther, Matthew G
Lazar, Mitchell A
Voelter, Wolfgang
Verdin, Eric
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2002-01
Volume: 9
Issue: 1
Pages: 45-57
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/s1097-2765(01)00429-4
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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Enzymatic Activity Associated with Class II HDACs Is Dependent on a Multiprotein Complex Containing HDAC3 and SMRT/N-CoR

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