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Background
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HDAC11 is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. The predominantly nuclear HDAC11, which interacts with HDAC6, is weakly expressed in most tissues, and strongly expressed in brain, heart, skeletal muscle, kidney and testis. Its activity is inhibited by trapoxin, a known histone deacetylase inhibitor.
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Background
References
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- Voelter-Mahlknecht S, et al., Int J Mol Med. 2005 Oct;16(4):589-98.
- Bradbury CA, et al., Leukemia. 2005 Oct;19(10):1751-9.
- Gregoretti IV, et al., J Mol Biol. 2004 Apr 16;338(1):17-31.
- Gao, L., et al., J. Biol. Chem. 277(28):25748-25755 (2002).
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