Evidence map›Paper›PMID 26450925›Full record

ArticleThe Biochemical journal2015

Histone deacetylase 3 indirectly modulates tubulin acetylation.

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

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.8field-weighted citation impact, top 28% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  11. Trichostatin A blocks aldosterone-induced NaBritish journal of pharmacology · 2019
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Travis BaconSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, U.K.
Caroline SeilerSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, U.K.
Marcin WolnySchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, U.K.
Ruth HughesSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, U.K.
Peter WatsonDepartment of Molecular and Cell Biology, Henry Wellcome Laboratories of Structural Biology, University of Leicester, Lancaster Road, Leicester LE1 9HN, U.K.
John SchwabeDepartment of Molecular and Cell Biology, Henry Wellcome Laboratories of Structural Biology, University of Leicester, Lancaster Road, Leicester LE1 9HN, U.K.
Ronald GriggSchool of Chemistry, Faculty of Maths and Physical Sciences, University of Leeds, Leeds LS2 9JT, U.K.
Michelle PeckhamSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, U.K. m.peckham@leeds.ac.uk.
University of Leeds · GBUniversity of Leicester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/I007423/1British Heart Foundation PG/15/2/31208Medical Research CouncilWellcome Trust 100237Wellcome Trust 100237/Z/12/ZWellcome Trust WT104918MA
6 · The paper itself

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.

Indexed as

AcetylationBenzamidesCell Line, TumorGene Knockdown TechniquesHistone Deacetylase 3Histone DeacetylasesHumansMicrotubulesNuclear Receptor Co-Repressor 2TubulinBenzamidesHistone Deacetylase 3Histone DeacetylasesMI-192NCOR2 protein, humanNuclear Receptor Co-Repressor 2Tubulinacetylationhistone deacetylase 3microtubulestubulin

Identifiers

PMID26450925
PMCPMC4661566
OpenAlexW2180646329

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.