Cited by 204Histone Deacetylase Inhibitors ResearchGenomics and Chromatin DynamicsEpigenetics and DNA Methylation

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Histone Deacetylase 3 Interacts with and Deacetylates Myocyte Enhancer Factor 2

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Grégoire, Serge, Xiao, Lin, Nie, Jianyun, Zhang, Xiaohong, Xu, Minghong, Li, Jiarong, Wong, Jiemin, Seto, Edward, Yang, Xiang-Jiao·2007·Molecular and Cellular Biology

DOI 10.1128/mcb.00882-06PMC PMC1800729

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Abstract

The myocyte enhancer factor 2 (MEF2) family of transcription factors is not only important for controlling gene expression in normal cellular programs, like muscle differentiation, T-cell apoptosis, neuronal survival, and synaptic differentiation, but has also been linked to cardiac hypertrophy and other pathological conditions. Lysine acetylation has been shown to modulate MEF2 function, but it is not so clear which deacetylase(s) is involved. We report here that treatment of HEK293 cells with trichostatin A or nicotinamide upregulated MEF2D acetylation, suggesting that different deacetylases catalyze the deacetylation. Related to the trichostatin A sensitivity, histone deacetylase 4 (HDAC4) and HDAC5, two known partners of MEF2, exhibited little deacetylase activity towards MEF2D. In contrast, HDAC3 efficiently deacetylated MEF2D in vitro and in vivo. This was specific, since HDAC1, HDAC2, and HDAC8 failed to do so. While HDAC4, HDAC5, HDAC7, and HDAC9 are known to recognize primarily the MEF2-specific domain, we found that HDAC3 interacts directly with the MADS box. In addition, HDAC3 associated with the acetyltransferases p300 and p300/CBP-associated factor (PCAF) to reverse autoacetylation. Furthermore, the nuclear receptor corepressor SMRT (silencing mediator of retinoid acid and thyroid hormone receptor) stimulated the deacetylase activity of HDAC3 towards MEF2 and PCAF. Supporting the physical interaction and deacetylase activity, HDAC3 repressed MEF2-dependent transcription and inhibited myogenesis. These results reveal an unexpected role for HDAC3 and suggest a novel pathway through which MEF2 activity is controlled in vivo.

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Authors: Grégoire, S., Xiao, L., Nie, J., Zhang, X., Xu, M., Li, J., Wong, J., Seto, E., & Yang, X.-J.
Affiliations: McGill University Health Centre (CA)
Moffitt Cancer Center (US)
Baylor College of Medicine (US)
Corresponding author: Yang, Xiang-Jiao
ORCID: Xiao, Lin
Zhang, Xiaohong
Li, Jiarong
Wong, Jiemin
Seto, Edward
Yang, Xiang-Jiao
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2007-02-01
Volume: 27
Issue: 4
Pages: 1280-1295
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.00882-06
PMC: PMC1800729
OpenAlex: W2170524079
Cited by: 203
References: 87
Citations by year: 2026: 3 · 2025: 8 · 2024: 7 · 2023: 4 · 2022: 9 · 2021: 4 · 2020: 12 · 2019: 6 · 2018: 7 · 2017: 10 · 2016: 9 · 2015: 12 · 2014: 12 · 2013: 15 · 2012: 12
FWCI: 5.04
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Cancer Institute
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, MEF2, MEF2D, lysine acetylation, protein deacetylation, MADS-box, P300, PCAF, SMRT, transcriptional repression, myogenesis, trichostatin A, nicotinamide, HDAC4, HDAC5
MeSH terms: Histone Deacetylase 3, p300-CBP-Associated Factor, Acetylation, Animals, Binding Sites, Histone Deacetylases, Humans, Models, Genetic, Nuclear Proteins, Protein Binding, Repressor Proteins, Transcription Factors, Transcription, Genetic, Protein Structure, Tertiary, Myogenic Regulatory Factors, Cell Cycle Proteins, Protein Transport, Muscle Development, Protein Interaction Mapping, Myoblasts, p300-CBP Transcription Factors, Mice, Histone Acetyltransferases, Nuclear Receptor Co-Repressor 1, MEF2 Transcription Factors

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Histone Deacetylase 3 Interacts with and Deacetylates Myocyte Enhancer Factor 2

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