期刊
BIOCHEMICAL JOURNAL
卷 472, 期 -, 页码 367-377出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20150660
关键词
acetylation; histone deacetylase 3; microtubules; tubulin
资金
- University of Leeds [Footsteps fund]
- Wellcome Trust [WT104918MA, WT100237]
- Biotechnology and Biological Sciences Research Council [BB/I007423/1]
- Royal Society
- BBSRC [BB/I007423/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/I007423/1] Funding Source: researchfish
- British Heart Foundation [PG/15/2/31208] Funding Source: researchfish
- Medical Research Council [1233630] Funding Source: researchfish
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. Abrief 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.
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