Evidence map›Paper›PMID 22890846›Full record

ArticleMolecular and cellular biology2012

A eukaryotic translation initiation factor 4E-binding protein promotes mRNA decapping and is required for PUF repression.

Nathan H Blewett, Aaron C Goldstrohm

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

46 citing papers in PubMed, 68 citations in OpenAlex.

  1. Med9 Is a Novel eIF4E-Interacting Protein inInternational journal of molecular sciences · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Regulation of theRNA (New York, N.Y.) · 2024
    Article
  8. Yeast Tor complex 1 phosphorylates eIF4E-binding protein, Caf20.Genes to cells : devoted to molecular & cellular mechanisms · 2023
    Article
  9. Article
  10. International journal of molecular sciences · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Lithium Chloride Sensitivity in Yeast and Regulation of Translation.International journal of molecular sciences · 2020
    Article
  16. Article
  17. eIF4E and Interactors from Unicellular Eukaryotes.International journal of molecular sciences · 2020
    Review
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Nathan H BlewettCellular and Molecular Biology Training Program, University of Michigan Medical School, Ann Arbor, Michigan, USA.
Aaron C Goldstrohm
University of Michigan–Ann Arbor · US

Funding

CELLULAR AND MOLECULAR BIOLOGY AT MICHIGANT32GM007315 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PUTHENVEEDU, MANOJKUMAR A · 1985 to 2021
$12.8M
NIGMS NIH HHS T32 GM007315NIGMS NIH HHS T32-GM007315
6 · The paper itself

Abstract

PUF proteins are eukaryotic RNA-binding proteins that repress specific mRNAs. The mechanisms and corepressors involved in PUF repression remain to be fully identified. Here, we investigated the mode of repression by Saccharomyces cerevisiae Puf5p and Puf4p and found that Puf5p specifically requires Eap1p to repress mRNAs, whereas Puf4p does not. Surprisingly, we observed that Eap1p, which is a member of the eukaryotic translation initiation factor 4E (eIF4E)-binding protein (4E-BP) class of translational inhibitors, does not inhibit the efficient polyribosome association of a Puf5p target mRNA. Rather, we found that Eap1p accelerates mRNA degradation by promoting decapping, and the ability of Eap1p to interact with eIF4E facilitates this activity. Deletion of EAP1 dramatically reduces decapping, resulting in accumulation of deadenylated, capped mRNA. In support of this phenotype, Eap1p associates both with Puf5p and the Dhh1p decapping factor. Furthermore, recruitment of Eap1p to downregulated mRNA is mediated by Puf5p. On the basis of these results, we propose that Puf5p promotes decapping by recruiting Eap1p and associated decapping factors to mRNAs. The implication of these findings is that a 4E-BP can repress protein expression by promoting specific mRNA degradation steps in addition to or in lieu of inhibiting translation initiation.

Indexed as

Down-RegulationEukaryotic Initiation Factor-4EPolyribosomesProtein BindingRNA-Binding ProteinsRNA CapsSaccharomyces cerevisiae ProteinsTranscription FactorsEap1 protein, S cerevisiaeEukaryotic Initiation Factor-4EMPT5 protein, S cerevisiaePUF4 protein, S cerevisiaeRNA-Binding ProteinsRNA CapsSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID22890846
PMCPMC3457345
OpenAlexW2156868329

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.