Histone deacetylase 3 indirectly modulates tubulin acetylation

Travis J Bacon, Caroline Seiler, Marcin Wolny, Ruth Hughes, Peter Watson, John Schwabe, Ronald Grigg, Michelle Peckham

Research output: Contribution to journalArticle (Academic Journal)peer-review

10 Citations (Scopus)
318 Downloads (Pure)

Abstract

Histone deacetylase 3 (HDAC3), a member of the Class I subfamily of HDACs, is found in both the nucleus and the cytoplasm. Its roles in the nucleus have been well characterized, but its cytoplasmic roles are still not elucidated fully. We found that blocking HDAC3 activity using MI192, a compound specific for HDAC3, modulated tubulin acetylation in the human prostate cancer cell line PC3. A brief 1 h treatment of PC3 cells with MI192 significantly increased levels of tubulin acetylation and ablated the dynamic behaviour of microtubules in live cells. siRNA-mediated knockdown (KD) of HDAC3 in PC3 cells, significantly increased levels of tubulin acetylation, and overexpression reduced it. However, the active HDAC3-silencing mediator of retinoic and thyroid receptors (SMRT)-deacetylase-activating domain (DAD) complex did not directly deacetylate tubulin in vitro. These data suggest that HDAC3 indirectly modulates tubulin acetylation.

Original languageEnglish
Pages (from-to)367-377
Number of pages11
JournalBiochemical Journal
Volume472
Issue number3
Early online date27 Nov 2015
DOIs
Publication statusPublished - 15 Dec 2015

Keywords

  • Acetylation
  • Benzamides
  • Cell Line, Tumor
  • Gene Knockdown Techniques
  • Histone Deacetylases
  • Humans
  • Microtubules
  • Nuclear Receptor Co-Repressor 2
  • Tubulin

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