Acetylation of histone deacetylase 6 by p300 attenuates its deacetylase activity

Han, Younho; Jeong, Hyun‐Dam; Jin, Yipeng; Kim, Yeon Jin; Jeong, Hye Gwang; Yeo, Chang Yeol; Lee, Kwang Youl

doi:10.1016/j.bbrc.2009.03.147

Cited by 46 publications

(42 citation statements)

References 25 publications

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“…HDACs, often directly compete for chromatin binding with KATs in a mutually exclusive manner [36]. Moreover, HDAC activity is attenuated by becoming acetylated itself by p300 [37], further demonstrating the KAT/HDAC relationship. Aberrant HDAC activity has been associated with many types of cancer [38] making both classical and sirtuin deacetylases important targets for therapeutics.…”

Section: Histone Lysine Deacetylationmentioning

confidence: 95%

Inhibitors of Enzymes Catalyzing Modifications to Histone Lysine Residues: Structure, Function and Activity

et al. 2016

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Gene expression is partly controlled by epigenetic mechanisms including histone-modifying enzymes. Some diseases are caused by changes in gene expression that can be mitigated by inhibiting histone-modifying enzymes. This review covers the enzyme inhibitors targeting histone lysine modifications. We summarize the enzymatic mechanisms of histone lysine acetylation, deacetylation, methylation and demethylation and discuss the biochemical roles of these modifications in gene expression and in disease. We discuss inhibitors of lysine acetylation, deacetylation, methylation and demethylation defining their structure-activity relationships and their potential mechanisms. We show that there are potentially indiscriminant off-target effects on gene expression even with the use of selective epigenetic enzyme inhibitors.

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Section: Histone Lysine Deacetylationmentioning

confidence: 95%

Inhibitors of Enzymes Catalyzing Modifications to Histone Lysine Residues: Structure, Function and Activity

et al. 2016

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“…Acetylation impairs HDAC6's activity against a-tubulin and transcriptional regulation [49]. Purified HDAC6 is acetylated at 16 lysine residues by the acetyltransferase p300 in vitro [8] (Figure 1A).…”

Section: Reviewmentioning

confidence: 99%

Drugging the HDAC6–HSP90 interplay in malignant cells

Krämer

Mahboobi

Sellmer

2014

Trends in Pharmacological Sciences

119

128

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“…Acetylation impairs HDAC6's activity against a-tubulin and transcriptional regulation [41,42]. Early studies have shown that acetyltransferase p300 acetylates HDAC6 at 16 lysine residues, leading to the inhibition of tubulin deacetylation and the suppression of Sp1 transcriptional activity (Fig.…”

Section: Sam68mentioning

confidence: 99%

Cellular defence or viral assist: the dilemma of HDAC6

Zheng

Jiang

et al. 2017

Journal of General Virology

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Histone deacetylase 6 (HDAC6) is a unique cytoplasmic deacetylase that regulates various important biological processes by preventing protein aggregation and deacetylating different non-histone substrates including tubulin, heat shock protein 90, cortactin, retinoic acid inducible gene I and b-catenin. Growing evidence has indicated a dual role for HDAC6 in viral infection and pathogenesis: HDAC6 may represent a host defence mechanism against viral infection by modulating microtubule acetylation, triggering antiviral immune response and stimulating protective autophagy, or it may be hijacked by the virus to enhance proinflammatory response. In this review, we will highlight current data illustrating the complexity and importance of HDAC6 in viral pathogenesis. We will summarize the structure and functional specificity of HDAC6, and its deacetylaseand ubiquitin-dependent activity in key cellular events in response to virus infection. We will also discuss how HDAC6 exerts its direct or indirect histone modification ability in viral lytic-latency switch.

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Acetylation of histone deacetylase 6 by p300 attenuates its deacetylase activity

Cited by 46 publications

References 25 publications

Inhibitors of Enzymes Catalyzing Modifications to Histone Lysine Residues: Structure, Function and Activity

Inhibitors of Enzymes Catalyzing Modifications to Histone Lysine Residues: Structure, Function and Activity

Drugging the HDAC6–HSP90 interplay in malignant cells

Cellular defence or viral assist: the dilemma of HDAC6

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