Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain

Tong, J. J.

doi:10.1093/nar/30.5.1114

Cited by 181Histone Deacetylase Inhibitors ResearchGenomics and Chromatin DynamicsEpigenetics and DNA Methylation

Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain

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Tong, J. J.·2002·Nucleic Acids Research

DOI 10.1093/nar/30.5.1114PMC PMC101247

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Abstract

Histone acetylation is important for regulating chromatin structure and gene expression. Three classes of mammalian histone deacetylases have been identified. Among class II, there are five known members, namely HDAC4, HDAC5, HDAC6, HDAC7 and HDAC9. Here we describe the identification and characterization of a novel class II member termed HDAC10. It is a 669 residue polypeptide with a bipartite modular structure consisting of an N-terminal Hda1p-related putative deacetylase domain and a C-terminal leucine-rich domain. HDAC10 is widely expressed in adult human tissues and cultured mammalian cells. It is enriched in the cytoplasm and this enrichment is not sensitive to leptomycin B, a specific inhibitor known to block the nuclear export of other class II members. The leucine-rich domain of HDAC10 is responsible for its cytoplasmic enrichment. Recombinant HDAC10 protein possesses histone deacetylase activity, which is sensitive to trichostatin A, a specific inhibitor for known class I and class II histone deacetylases. When tethered to a promoter, HDAC10 is able to repress transcription. Furthermore, HDAC10 interacts with HDAC3 but not with HDAC4 or HDAC6. These results indicate that HDAC10 is a novel class II histone deacetylase possessing a unique leucine-rich domain.

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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 [19]
HDAC10 is enriched in the cytoplasm.
“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 [19]
The ΨDAC domain of HDAC10 has no known catalytic function, although it may play a role in directing cytoplasmic enrichment.
“The ΨDAC domain of HDAC10 has no known catalytic function, although it may play a role in directing cytoplasmic enrichment19.”
From Histone deacetylase 10 structure and molecular function as a polyamine deacetylase (2017) · cites this paper as [19]

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Osbourn, A. (2004) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1017097.202490

Authors: Tong, J. J.
Affiliations: McGill University Health Centre (CA)
Corresponding author: Tong, J. J.
ORCID: Tong, J. J.
Venue: Nucleic Acids Research
Publisher: Oxford University Press (OUP)
Published: 2002-03-01
Volume: 30
Issue: 5
Pages: 1114-1123
ISSN: 0305-1048 (ISSN-L)
1362-4962
DOI: 10.1093/nar/30.5.1114
PMC: PMC101247
OpenAlex: W2104210885
Cited by: 181
References: 81
Citations by year: 2026: 3 · 2025: 8 · 2024: 16 · 2023: 14 · 2022: 11 · 2021: 10 · 2020: 10 · 2019: 6 · 2018: 6 · 2017: 7 · 2016: 2 · 2015: 9 · 2014: 6 · 2013: 5 · 2012: 6
FWCI: 3.24
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Nucleic Acids Research (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Cancer Institute
Solar Energy Technologies Office
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 histone deacetylases, leucine-rich domain, histone acetylation, chromatin structure, transcriptional repression, cytoplasmic localization, gene expression regulation
MeSH terms: Amino Acid Sequence, Animals, Cell Line, Cloning, Molecular, Cytoplasm, HeLa Cells, Histone Deacetylases, Humans, Leucine, Molecular Sequence Data, Repressor Proteins, RNA, Messenger, Tissue Distribution, Transcription, Genetic, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Genes, Reporter, Mice, Rats

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Identification of HDAC10, a novel class II human histone deacetylase containing a leucine-rich domain

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