Evidence map›Paper›PMID 20532201›Full record

ArticlePLoS genetics2010

14-3-3 mediates histone cross-talk during transcription elongation in Drosophila.

Caline S Karam, Wendy A Kellner, Naomi Takenaka, Alexa W Clemmons, Victor G Corces

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
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  5. Review
  6. Article
  7. Elongator complex is required for long-term olfactory memory formation inLearning & memory (Cold Spring Harbor, N.Y.) · 2018
    Article
  8. Article
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  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Histone regulation in the CNS: basic principles of epigenetic plasticity.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2013
    Review
  19. Review
  20. Article
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

5 authors at 1 institution in 1 country.

Caline S KaramDepartment of Biology, Emory University, Atlanta, Georgia, United States of America.
Wendy A Kellner
Naomi Takenaka
Alexa W Clemmons
Victor G Corces
Emory University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modifications of histone proteins modulate the binding of transcription regulators to chromatin. Studies in Drosophila have shown that the phosphorylation of histone H3 at Ser10 (H3S10ph) by JIL-1 is required specifically during early transcription elongation. 14-3-3 proteins bind H3 only when phosphorylated, providing mechanistic insights into the role of H3S10ph in transcription. Findings presented here show that 14-3-3 functions downstream of H3S10ph during transcription elongation. 14-3-3 proteins localize to active genes in a JIL-1-dependent manner. In the absence of 14-3-3, levels of actively elongating RNA polymerase II are severely diminished. 14-3-3 proteins interact with Elongator protein 3 (Elp3), an acetyltransferase that functions during transcription elongation. JIL-1 and 14-3-3 are required for Elp3 binding to chromatin, and in the absence of either protein, levels of H3K9 acetylation are significantly reduced. These results suggest that 14-3-3 proteins mediate cross-talk between histone phosphorylation and acetylation at a critical step in transcription elongation.

Indexed as

Transcription, Genetic14-3-3 ProteinsAcetylationAnimalsChromosomesDrosophila melanogasterDrosophila ProteinsGene Expression RegulationHistone AcetyltransferasesHistonesNerve Tissue ProteinsPhosphorylationProtein BindingProtein Processing, Post-TranslationalProtein Serine-Threonine Kinases14-3-3 ProteinsDrosophila ProteinsELP3 protein, DrosophilaHistone AcetyltransferasesHistonesJIL-1 protein, DrosophilaNerve Tissue ProteinsProtein Serine-Threonine Kinases

Identifiers

PMID20532201
PMCPMC2880557
OpenAlexW2080668421

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.