Evidence map›Paper›PMID 27798844›Full record

ArticleGenes & development2016

Post-transcriptional control of executioner caspases by RNA-binding proteins.

Deni Subasic, Thomas Stoeger, Seline Eisenring, Ana M Matia-González, Jochen Imig, Xue Zheng, Lei Xiong, Pascal Gisler, Ralf Eberhard, René Holtackers and 3 more

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. Cell death in animal development.Development (Cambridge, England) · 2020
    Review
  6. 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

13 authors at 3 institutions in 2 countries.

Deni SubasicInstitute of Molecular Life Sciences, University of Zurich, 8057 Zurich, Switzerland.
Thomas StoegerInstitute of Molecular Life Sciences, University of Zurich, 8057 Zurich, Switzerland.
Seline EisenringInstitute of Molecular Life Sciences, University of Zurich, 8057 Zurich, Switzerland.
Ana M Matia-GonzálezFaculty of Health and Medical Sciences, Department of Microbial and Cellular Sciences, University of Surrey, Stag Hill Campus, GU2 7XH Guildford, United Kingdom.
Jochen ImigInstitute of Pharmaceutical Sciences, Swiss Federal Institute of Technology, 8093 Zurich, Switzerland.
Xue ZhengInstitute of Molecular Life Sciences, University of Zurich, 8057 Zurich, Switzerland.
Lei XiongInstitute of Molecular Life Sciences, University of Zurich, 8057 Zurich, Switzerland.
Pascal GislerInstitute of Molecular Life Sciences, University of Zurich, 8057 Zurich, Switzerland.
Ralf EberhardInstitute of Molecular Life Sciences, University of Zurich, 8057 Zurich, Switzerland.
René HoltackersInstitute of Molecular Life Sciences, University of Zurich, 8057 Zurich, Switzerland.
André P GerberFaculty of Health and Medical Sciences, Department of Microbial and Cellular Sciences, University of Surrey, Stag Hill Campus, GU2 7XH Guildford, United Kingdom.
Lucas PelkmansInstitute of Molecular Life Sciences, University of Zurich, 8057 Zurich, Switzerland.
Michael O HengartnerInstitute of Molecular Life Sciences, University of Zurich, 8057 Zurich, Switzerland.
University of Zurich · CHÉcole Polytechnique Fédérale de Lausanne · CHUniversity of Surrey · GB

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Ann E. Rougvie · 2012 to 2026
$7.5M
NIH HHS P40 OD010440
6 · The paper itself

Abstract

Caspases are key components of apoptotic pathways. Regulation of caspases occurs at several levels, including transcription, proteolytic processing, inhibition of enzymatic function, and protein degradation. In contrast, little is known about the extent of post-transcriptional control of caspases. Here, we describe four conserved RNA-binding proteins (RBPs)-PUF-8, MEX-3, GLD-1, and CGH-1-that sequentially repress the CED-3 caspase in distinct regions of the Caenorhabditis elegans germline. We demonstrate that GLD-1 represses ced-3 mRNA translation via two binding sites in its 3' untranslated region (UTR), thereby ensuring a dual control of unwanted cell death: at the level of p53/CEP-1 and at the executioner caspase level. Moreover, we identified seven RBPs that regulate human caspase-3 expression and/or activation, including human PUF-8, GLD-1, and CGH-1 homologs PUM1, QKI, and DDX6. Given the presence of unusually long executioner caspase 3' UTRs in many metazoans, translational control of executioner caspases by RBPs might be a strategy used widely across the animal kingdom to control apoptosis.

Indexed as

Gene Expression Regulation, Developmental3' Untranslated RegionsAnimalsApoptosisBinding SitesCaenorhabditis elegansCaenorhabditis elegans ProteinsCaspasesGerm CellsHeLa CellsHumansRNA-Binding ProteinsRNA Processing, Post-Transcriptional3' Untranslated RegionsCaenorhabditis elegans ProteinsCaspasesRNA-Binding Proteinsapoptosiscaspasecaspase-3CED-3GLD-1RNA-binding proteinstranslational control

Identifiers

PMID27798844
PMCPMC5088569
OpenAlexW2538151246

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.