The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Functional Domains of Histone Deacetylase-3
Open accessAbstract
Post-translational modifications of histones, in general, and acetylation/deacetylation, in particular, can dramatically alter gene expression in eukaryotic cells. In humans, four highly homologous class I HDAC enzymes (HDAC1, HDAC2, HDAC3, and HDAC8) have been identified to date. Although HDAC3 shares some structural and functional similarities with other class I HDACs, it exists in multisubunit complexes separate and different from other known HDAC complexes, implying that individual HDACs might function in a distinct manner. In this current study, to understand further the cellular function of HDAC3 and to uncover possible unique roles this protein may have in gene regulation, we performed a detailed analysis of HDAC3 using deletion mutations. Surprisingly, we found that the non-conserved C-terminal region of HDAC3 is required for both deacetylase and transcriptional repression activity. In addition, we discovered that the central portion of the HDAC3 protein possesses a nuclear export signal, whereas the C-terminal part of HDAC3 contributes to the protein's localization in the nucleus. Finally, we found that HDAC3 forms oligomers in vitro and in vivo and that the N-terminal portion of HDAC3 is necessary for this property. These data indicate that HDAC3 comprises separate, non-overlapping domains that contribute to the unique properties and function of this protein.
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Cited by
Histone deacetylases (HDACs): characterization of the classical HDAC family
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Stat3 Dimerization Regulated by Reversible Acetylation of a Single Lysine Residue
Yuan, Z.-L., Guan, Y.-J., Chatterjee, D., & Chin, Y. E. (2005) · Science · doi:10.1126/science.1105166 · Cited by 790
HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics
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Histone deacetylases as regulators of inflammation and immunity
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Metadata
- Authors
- Yang, W.-M., Tsai, S.-C., Wen, Y.-D., Fejér, G., & Seto, E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-03
- Volume
- 277
- Issue
- 11
- Pages
- 9447-9454
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2084194105
- Cited by
- 248
- References
- 15
- FWCI
- 3.13
- Type
- journal article
- Language
- en
- Open access
- hybrid
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