Isolation and Characterization of Mammalian HDAC10, a Novel Histone Deacetylase
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Acetylation of histone core particles plays an important role in modulating chromatin structure and gene expression. The acetylation status of the histone tails is determined by two opposing enzymatic activities, histone acetyltransferases and histone deacetylases (HDACs). Here we describe the isolation and characterization of HDAC10, a novel class II histone deacetylase. Molecular cloning and Northern blot analyses reveal that the HDAC10 transcript is widely expressed and subjected to alternative splicing. HDAC10 is both nuclear and cytoplasmic, a feature reminiscent of HDACs 4, 5, and 7. Distinct from other family members, HDAC10 harbors an amino-terminal catalytic domain and a carboxyl pseudo-repeat that shares significant homology with its catalytic domain. Mutational analysis reveals that transcriptional repression by HDAC10 requires its intrinsic histone deacetylase activity. Taken together, HDAC10 represents a distinct HDAC that may play a role in transcription regulation.
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HDAC10 is highly expressed in the liver, spleen and kidney.
“HDAC10 is highly expressed in the liver, spleen and kidney1819, enriched in the cytoplasm19 and resistant to inhibition by sodium butyrate20.”
From Histone deacetylase 10 structure and molecular function as a polyamine deacetylase (2017) · cites this paper as [18]
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- Authors
- Kao, H.-Y., Lee, C.-H., Komarov, A., Han, C. C., & Evans, R. M.
- Affiliations
- University Hospitals of Cleveland (US)
- Salk Institute for Biological Studies (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-01
- Volume
- 277
- Issue
- 1
- Pages
- 187-193
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1996507777
- Cited by
- 193
- References
- 53
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 5 · 2023: 12 · 2022: 4 · 2021: 10 · 2020: 13 · 2019: 9 · 2018: 5 · 2017: 4 · 2016: 6 · 2015: 8 · 2014: 10 · 2013: 7 · 2012: 7
- FWCI
- 5.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R01HD027183, HD-27183)
- 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
- HDAC10, histone deacetylase, class II HDACs, histone acetylation, chromatin structure, transcriptional repression, alternative splicing, nuclear-cytoplasmic localization, catalytic domain, gene expression
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Cell Nucleus, Cytoplasm, Histone Deacetylases, Humans, Molecular Sequence Data, Transcription, Genetic, DNA, Complementary, Mice
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