Evidence map›Paper›PMID 24607507›Full record

ArticleBiochimica et biophysica acta2014

RNAi screen in Drosophila larvae identifies histone deacetylase 3 as a positive regulator of the hsp70 heat shock gene expression during heat shock.

Bhavana G Achary, Katie M Campbell, Ivy S Co, David S Gilmour

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
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    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

4 authors at 1 institution in 1 country.

Bhavana G AcharyDepartment of Biochemistry and Molecular Biology, Center for Eukaryotic Gene Regulation, Pennsylvania State University, University Park, PA 16802, USA.
Katie M CampbellDepartment of Biochemistry and Molecular Biology, Center for Eukaryotic Gene Regulation, Pennsylvania State University, University Park, PA 16802, USA.
Ivy S CoDepartment of Biochemistry and Molecular Biology, Center for Eukaryotic Gene Regulation, Pennsylvania State University, University Park, PA 16802, USA.
David S GilmourDepartment of Biochemistry and Molecular Biology, Center for Eukaryotic Gene Regulation, Pennsylvania State University, University Park, PA 16802, USA. Electronic address: dsg11@psu.edu.
Pennsylvania State University · US

Funding

POTENTIATED STATE OF THE HSP70 HEAT SHOCK GENER01GM047477 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI GILMOUR, DAVID SCOTT · 1992 to 2022
$6.7M
NIGMS NIH HHS GM47477NIGMS NIH HHS R01 GM047477
6 · The paper itself

Abstract

The transcription regulation of the Drosophila hsp70 gene is a complex process that involves the regulation of multiple steps, including the establishment of paused Pol II and release of Pol II into elongation upon heat shock activation. While the major players involved in the regulation of gene expression have been studied in detail, additional factors involved in this process continue to be discovered. To identify factors involved in hsp70 expression, we developed a screen that capitalizes on a visual assessment of heat shock activation using a hsp70-beta galactosidase reporter and publicly available RNAi fly lines to deplete candidate proteins. We validated the screen by showing that the depletion of HSF, CycT, Cdk9, Nurf 301, or ELL prevented the full induction of hsp70 by heat shock. Our screen also identified the histone deacetylase HDAC3 and its associated protein SMRTER as positive regulators of hsp70 activation. Additionally, we show that HDAC3 and SMRTER contribute to hsp70 gene expression at a step subsequent to HSF-mediated activation and release of the paused Pol II that resides at the promoter prior to heat shock induction.

Indexed as

Gene Expression RegulationRNA InterferenceAnimalsDNA-Binding ProteinsDrosophilaDrosophila ProteinsGene ExpressionHeat-Shock ResponseHistone Deacetylase 3Histone DeacetylasesHot TemperatureHSP70 Heat-Shock ProteinsLarvaRNA Polymerase IITranscription FactorsTransgenesDNA-Binding ProteinsDrosophila ProteinsHistone Deacetylase 3Histone DeacetylasesHSP70 Heat-Shock ProteinsRNA Polymerase IITranscription FactorsHDAC3Heat shockhsp70RNA polymerase IISMRTERTranscription

Identifiers

PMID24607507
PMCPMC4013238
OpenAlexW1996893979

What OpenQuestion holds

Textmetadata
LicenceTDM
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.