HDAC8 deacetylates histones

Stable Identifier
Reaction [transition]
Homo sapiens
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HDAC8 can catalyze the in vitro deacetylation of a number of acetylated histone variants including full-length H2A/H2B, H3, and H4 histones acetylated at nonspecific lysines (Hu et al. 2000, Buggy et al. 2000). Peptide sequences corresponding to the H4 histone tail with an acetylated lysine at position sixteen (AcK16) were also identified as in vitro substrates (Buggy et al. 2000, Van der Wyngaert et al. 2000). Subsequent studies have used the H4 histone tail sequence as a peptide template to investigate the amino acid sequence preference of HDAC8. HDAC8 can catalyze the in vitro deacetylation of AcK20 on the H4 histone tail though at a much slower rate than deacetylation of AcK16 peptides (Dose et al. 2011). HDAC8 can catalyze deacetylation in vivo in the absence of a protein complex (Dowling et al. 2010). The role of HDAC8 in catalyzing deacetylation of specific sites in histones in vivo remains unclear (Wolfson et al. 2013).

Literature References
PubMed ID Title Journal Year
10926844 Cloning and characterization of a novel human histone deacetylase, HDAC8

McIntosh, B, Mak, P, Clark, JM, Lorimer, DD, Buggy, JJ, Sideris, ML

Biochem. J. 2000
10748112 Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor

Hu, E, Zhu, Y, Fredrickson, T, Winkler, J, Chen, Z, Kirkpatrick, R, Liu, R, Johanson, K, Zhang, GF, Sung, CM

J. Biol. Chem. 2000
Catalyst Activity

histone deacetylase activity of HDAC8 [nucleoplasm]

Orthologous Events
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