Evidence map›Paper›PMID 12917335›Full record

ArticleMolecular and cellular biology2003

Protein phosphatase 2A activity affects histone H3 phosphorylation and transcription in Drosophila melanogaster.

Scott J Nowak, Chi-Yun Pai, Victor G Corces

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

38 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Ser/Thr phosphatases: One of the key regulators of insulin signaling.Reviews in endocrine & metabolic disorders · 2022
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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

3 authors at 1 institution in 1 country.

Scott J NowakDepartment of Biology, The Johns Hopkins University, Baltimore, Maryland 21218, USA.
Chi-Yun Pai
Victor G Corces
Johns Hopkins University · US

Funding

MOLECULAR BASIS OF SUPPRESSION IN DROSOPHILAR01GM035463 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CORCES, VICTOR G. · 1986 to 2020
$10.7M
NIGMS NIH HHS GM35463NIGMS NIH HHS R01 GM035463
6 · The paper itself

Abstract

Transcriptional activation of the heat shock genes during the heat shock response in Drosophila has been intimately linked to phosphorylation of histone H3 at serine 10, whereas repression of non-heat-shock genes correlates with dephosphorylation of histone H3. It is then possible that specific kinase and/or phosphatase activities may regulate histone phosphorylation and therefore transcription activation and repression, respectively. We find that treatment of cells with strong phosphatase inhibitors interferes with the genome-wide dephosphorylation of histone H3 normally observed at non-heat-shock genes during heat shock. Mutants in protein phosphatase type 2A (PP2A) also display reduced genome-wide H3 dephosphorylation, and sites of H3 phosphorylation that do not contain heat shock genes remain transcriptionally active during heat shock in PP2A mutants. Finally, the SET protein, a potent and highly selective inhibitor of PP2A activity that inhibits PP2A-mediated dephosphorylation of Ser10-phosphorylated H3, is detected at transcriptionally active regions of polytene chromosomes. These results suggest that activation and repression of gene expression during heat shock might be regulated by changes in PP2A activity controlled by the SET protein.

Indexed as

Transcription, GeneticAnimalsChromosomal Proteins, Non-HistoneDrosophila melanogasterDrosophila ProteinsEnzyme InhibitorsGene Expression RegulationHeat-Shock ResponseHistonesLarvaMutationOkadaic AcidPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 2ProteinsChromosomal Proteins, Non-HistoneDrosophila ProteinsEnzyme InhibitorsHistonesOkadaic AcidPhosphoprotein PhosphatasesProtein Phosphatase 2ProteinsRNA Polymerase IISerineTranscription Factors

Identifiers

PMID12917335
PMCPMC180939
OpenAlexW2126014610

What OpenQuestion holds

Textmetadata
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.