Evidence map›Paper›PMID 22932903›Full record

ArticleThe Journal of biological chemistry2012

dTIS11 Protein-dependent polysomal deadenylation is the key step in AU-rich element-mediated mRNA decay in Drosophila cells.

Caroline Vindry, Aurélien Lauwers, David Hutin, Romuald Soin, Corinne Wauquier, Véronique Kruys, Cyril Gueydan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The role of RNA-binding protein tristetraprolin in cancer and immunity.Medical oncology (Northwood, London, England) · 2017
    Review
  7. Review
  8. Exaptive origins of regulated mRNA decay in eukaryotes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016
    Review
  9. Article
  10. RNA binding proteins as regulators of immune cell biology.Clinical and experimental immunology · 2016
    Review
  11. Article
  12. Review
  13. Article
  14. Review
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

7 authors at 1 institution in 1 country.

Caroline VindryLaboratoire de Biologie Moléculaire du Gène, Université Libre de Bruxelles, 12 rue Pr. Jeener et Brachet, 6041 Gosselies, Belgium.
Aurélien LauwersLaboratoire de Biologie Moléculaire du Gène, Université Libre de Bruxelles, 12 rue Pr. Jeener et Brachet, 6041 Gosselies, Belgium.
David HutinLaboratoire d'Immunobiologie, Université Libre de Bruxelles, 12 rue Pr. Jeener et Brachet, 6041 Gosselies, Belgium.
Romuald SoinLaboratoire de Biologie Moléculaire du Gène, Université Libre de Bruxelles, 12 rue Pr. Jeener et Brachet, 6041 Gosselies, Belgium.
Corinne WauquierLaboratoire de Biologie Moléculaire du Gène, Université Libre de Bruxelles, 12 rue Pr. Jeener et Brachet, 6041 Gosselies, Belgium.
Véronique KruysLaboratoire de Biologie Moléculaire du Gène, Université Libre de Bruxelles, 12 rue Pr. Jeener et Brachet, 6041 Gosselies, Belgium; Center for Microscopy and Molecular Imaging, Faculté des Sciences, Université Libre de Bruxelles, 12 rue Pr. Jeener et Brachet, 6041 Gosselies, Belgium.
Cyril GueydanLaboratoire de Biologie Moléculaire du Gène, Université Libre de Bruxelles, 12 rue Pr. Jeener et Brachet, 6041 Gosselies, Belgium. Electronic address: cgueydan@ulb.ac.be.
Université Libre de Bruxelles · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The destabilization of AU-rich element (ARE)-containing mRNAs mediated by proteins of the TIS11 family is conserved among eukaryotes including Drosophila. Previous studies have demonstrated that Tristetraprolin, a human protein of the TIS11 family, induces the degradation of ARE-containing mRNAs through a large variety of mechanisms including deadenylation, decapping, and P-body targeting. We have previously shown that the degradation of the mRNA encoding the antimicrobial peptide Cecropin A1 (CecA1) is controlled by the TIS11 protein (dTIS11) in Drosophila cells. In this study, we used CecA1 mRNA as a model to investigate the molecular mechanism of dTIS11-mediated mRNA decay. We observed that during the biphasic deadenylation and decay process of this mRNA, dTIS11 enhances deadenylation performed by the CCR4-CAF-NOT complex while the mRNA is still associated with ribosomes. Sequencing of mRNA degradation intermediates revealed that the complete deadenylation of the mRNA triggers its decapping and decay in both the 5'-3' and the 3'-5' directions. Contrary to the observations made for its mammalian homologs, overexpression of dTIS11 does not promote the localization of ARE-containing mRNAs in P-bodies but rather decreases the accumulation of CecA1 mRNA in these structures by enhancing the degradation process. Therefore, our results suggest that proteins of the TIS11 family may have acquired additional functions in the course of evolution from invertebrates to mammals.

Indexed as

AnimalsAntimicrobial Cationic PeptidesAU Rich ElementsCell LineDrosophila melanogasterDrosophila ProteinsEvolution, MolecularHumansRibonucleasesRNA-Binding ProteinsRNA, MessengerRNA StabilityTristetraprolinAntimicrobial Cationic PeptidesCCR4 protein, Drosophilacecropin ADrosophila ProteinsRibonucleasesRNA-Binding ProteinsRNA, MessengerTis11 protein, DrosophilaTristetraprolinZFP36 protein, human

Identifiers

PMID22932903
PMCPMC3471692
OpenAlexW2016674854

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.