The DOI matches its Crossref record; 86 of the 87 references it cites were found in a registry or an index.
Histone Deacetylase 3 Interacts with and Deacetylates Myocyte Enhancer Factor 2
Open accessAbstract
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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“More recently, it has been shown that both Sirt1 (28) and HDAC3 (29), and not HDAC4 or -5, efficiently deacetylate MEF2D, thus contributing to MEF2Ddependent transcriptional repression.”
From Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases (2007) · cites this paper as [29]
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The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases
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hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,690
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403
Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081
Acetylation of Histones and Transcription-Related Factors
Sterner, D. E., & Berger, S. L. (2000) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.64.2.435-459.2000 · Cited by 1,824
A transcriptional co-repressor that interacts with nuclear hormone receptors
Chen, J. D., & Evans, R. M. (1995) · Nature · doi:10.1038/377454a0 · Cited by 1,794
The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase
North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., & Verdin, E. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00038-8 · Cited by 1,542
A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
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Self-citationThe Sir2 Family of Protein Deacetylases
Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,497
Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey
Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.026 · Cited by 1,487
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Enzymatic Mechanisms and Chemical Probes of the Myst Family of Histone Acetyltransferases
Yang, C. (2022) · Digital Archive @ GSU · doi:10.57709/4313955
Combining heterogeneous sources of data for the reverse-engineering of gene regulatory networks
Steele, E. (2010) · Brunel University Research Archive (BURA) (Brunel University London)
Histone acetylation modulates uncoupling protein1 expression in brown adipocytes
Rajan, A. (2022) · Digital Archive @ GSU · doi:10.57709/5582376
Metadata
- 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
- 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
- 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
- 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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