Evidence map›Paper›PMID 19682251›Full record

ArticleMolecular microbiology2009

Enhancer of decapping proteins 1 and 2 are important for translation during heat stress in Saccharomyces cerevisiae.

Daniel W Neef, Dennis J Thiele

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. International journal of molecular sciences · 2023
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. mRNA decapping: finding the right structures.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. mTOR signaling in protein homeostasis: less is more?Cell cycle (Georgetown, Tex.) · 2011
    Review
  14. Article
  15. Article
  16. Article
  17. 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

2 authors at 1 institution in 1 country.

Daniel W NeefDepartment of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.
Dennis J Thiele
Duke University Hospital · US

Funding

HEAT SHOCK TRANSCRIPTION FACTOR FUNCTION AND REGULATIONR01GM059911 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI THIELE, DENNIS J. · 1999 to 2007
$2.2M
Stress regulation of RNA metabolismF32GM076954 · NIGMS · DUKE UNIVERSITY · PI NEEF, DANIEL W · 2006 to 2008
$99k
NIGMS NIH HHS F32 GM076954NIGMS NIH HHS GM076954NIGMS NIH HHS R01 GM059911NIGMS NIH HHS R01-GM059911
6 · The paper itself

Abstract

In mammalian and Drosophila cells, heat stress strongly reduces general protein translation while activating cap-independent translation mechanisms to promote the expression of stress-response proteins. In contrast, in Saccharomyces cerevisiae general translation is only mildly and transiently reduced by heat stress and cap-independent translation mechanisms have not been correlated with the heat stress response. Recently we have identified direct target genes of the heat shock transcription factor (HSF), including genes encoding proteins thought to be important for general translation. One gene activated by HSF during heat stress encodes the enhancer of decapping protein, Edc2, previously shown to enhance mRNA decapping under conditions when the decapping machinery is limited. In this report we show that strains lacking Edc2, as well as the paralogous protein Edc1, are compromised for growth under persistent heat stress. This growth deficiency can be rescued by expression of a mutant Edc1 protein deficient in mRNA decapping indicative of a decapping independent function during heat stress. Yeast strains lacking Edc1 and Edc2 are also sensitive to the pharmacological inhibitor of translation paromomycin and exposure to heat stress and paromomycin functions synergistically to reduce yeast viability, suggesting that in the absence of Edc1 and Edc2 translation is compromised under heat stress conditions. Strains lacking Edc1 and Edc2 have significantly reduced rates of protein translation during growth under heat stress conditions, but not under normal growth conditions. We propose that Edc1 and the stress responsive isoform Edc2 play important roles in protein translation during stress.

Indexed as

Hot TemperatureProtein BiosynthesisStress, PhysiologicalAntifungal AgentsGene Knockout TechniquesParomomycinRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAntifungal AgentsEdc1 protein, S cerevisiaeEdc2 protein, S cerevisiaeParomomycinRNA-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID19682251
PMCPMC2901857
OpenAlexW2096405334

What OpenQuestion holds

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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.