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Title: Histone deacetylase 3 indirectly modulates tubulin acetylation
Authors: Bacon, T.
Seiler, C.
Wolny, M.
Hughes, R.
Watson, P. C.
Schwabe, John W. R.
Grigg, R.
Peckham, M.
First Published: 27-Nov-2015
Publisher: Portland Press for Biochemical Society
Citation: Biochemical Journal, 2015, 472 (3), pp. 367-377
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.
DOI Link: 10.1042/BJ20150660
ISSN: 0264-6021
eISSN: 1470-8728
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © 2015 Authors. This is an open access article published by Portland Press Limited and distributed under the Creative Commons Attribution License 3.0 ( ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Appears in Collections:Published Articles, College of Medicine, Biological Sciences and Psychology

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