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Molecular Cloning and Characterization of a Novel Histone Deacetylase HDAC10
Open accessAbstract
The growing number of proteins controlled by reversible acetylation suggests the existence of a large number of acetyltransferases and deacetylases. Here, we report the identification of a novel class II histone deacetylase, HDAC10. Homology comparison indicates that HDAC10 is most similar to HDAC6. Both contain a unique, putative second catalytic domain not found in other HDACs. In HDAC10, however, this domain is not functional. This tandem organization of two catalytic domains confers resistance to the inhibitors trapoxin B and sodium butyrate, which potently inhibit the deacetylase activity of all other HDAC members. Thus, HDAC10 and HDAC6 share unusual structural and pharmacological characteristics. However, unlike HDAC6, which is normally a cytoplasmic deacetylase, HDAC10 resides in both the nucleus and cytoplasm. In the nucleus, when tethered to a promoter, HDAC10 represses transcription independent of its deacetylase activity, indicating that HDAC10 contains a distinct transcriptional repressor domain. These observations suggest that HDAC10 might uniquely play roles both in the nucleus, as a transcriptional modulator, and in the cytoplasm in an unidentified role. Together, our results identify HDAC10 as a novel deacetylase with distinct structure, pharmacology and localization and further expand the complexity of the HDAC family.
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“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 [20]
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Histone deacetylases (HDACs): characterization of the classical HDAC family
RUIJTER, A. J. M. D., GENNIP, A. H. V., CARON, H. N., KEMP, S., & KUILENBURG, A. B. P. V. (2003) · Biochemical Journal · doi:10.1042/bj20021321 · Cited by 3,114
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HDAC6 is a microtubule-associated deacetylase
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Self-citationHDAC2 negatively regulates memory formation and synaptic plasticity
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Metadata
- Authors
- Guardiola, A. R., & Yao, T.-P.
- Affiliations
- Duke Medical Center (US)
- Corresponding author
- Yao, Tso-Pang
- ORCID
- Yao, Tso-Pang
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-02
- Volume
- 277
- Issue
- 5
- Pages
- 3350-3356
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1987366741
- Cited by
- 253
- References
- 30
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 7 · 2023: 10 · 2022: 10 · 2021: 16 · 2020: 10 · 2019: 5 · 2018: 9 · 2017: 9 · 2016: 3 · 2015: 11 · 2014: 11 · 2013: 8 · 2012: 13
- FWCI
- 5.56
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Damon Runyon Cancer Research Foundation
- 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, HDAC6, transcriptional repression, nuclear localization, cytoplasmic localization, histone acetylation, deacetylase inhibitors
- MeSH terms
- Histone Deacetylase 6, Amino Acid Sequence, Cell Line, Chromosome Mapping, Chromosomes, Human, Pair 22, Cloning, Molecular, Gene Expression Regulation, Histone Deacetylases, Humans, Molecular Sequence Data, Phylogeny, Recombinant Proteins, Repressor Proteins, Transcription, Genetic, Transfection, Polymerase Chain Reaction, Sequence Alignment, Sequence Homology, Amino Acid, DNA Primers, Catalytic Domain
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