Evidence map›Paper›PMID 10848587›Full record

ArticleMolecular and cellular biology2000

Eap1p, a novel eukaryotic translation initiation factor 4E-associated protein in Saccharomyces cerevisiae.

G P Cosentino, T Schmelzle, A Haghighat, S B Helliwell, M N Hall, N Sonenberg

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

55 citing papers in PubMed, 130 citations in OpenAlex.

  1. Med9 Is a Novel eIF4E-Interacting Protein inInternational journal of molecular sciences · 2026
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  2. Article
  3. Article
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  5. Yeast Tor complex 1 phosphorylates eIF4E-binding protein, Caf20.Genes to cells : devoted to molecular & cellular mechanisms · 2023
    Article
  6. Article
  7. International journal of molecular sciences · 2023
    Article
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  9. Article
  10. Review
  11. Article
  12. Vps34 and TOR Kinases CoordinateMolecular and cellular biology · 2021
    Article
  13. Article
  14. eIF4E and Interactors from Unicellular Eukaryotes.International journal of molecular sciences · 2020
    Review
  15. Article
  16. Review
  17. Article
  18. 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

6 authors at 3 institutions in 2 countries.

G P CosentinoDepartment of Biochemistry and McGill Cancer Center, McGill University, Montreal, Québec H3G 1Y6, Canada.
T Schmelzle
A Haghighat
S B Helliwell
M N Hall
N Sonenberg
University of Basel · CHMcGill University · CABoehringer Ingelheim (Canada) · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosome binding to eukaryotic mRNA is a multistep process which is mediated by the cap structure [m(7)G(5')ppp(5')N, where N is any nucleotide] present at the 5' termini of all cellular (with the exception of organellar) mRNAs. The heterotrimeric complex, eukaryotic initiation factor 4F (eIF4F), interacts directly with the cap structure via the eIF4E subunit and functions to assemble a ribosomal initiation complex on the mRNA. In mammalian cells, eIF4E activity is regulated in part by three related translational repressors (4E-BPs), which bind to eIF4E directly and preclude the assembly of eIF4F. No structural counterpart to 4E-BPs exists in the budding yeast, Saccharomyces cerevisiae. However, a functional homolog (named p20) has been described which blocks cap-dependent translation by a mechanism analogous to that of 4E-BPs. We report here on the characterization of a novel yeast eIF4E-associated protein (Eap1p) which can also regulate translation through binding to eIF4E. Eap1p shares limited homology to p20 in a region which contains the canonical eIF4E-binding motif. Deletion of this domain or point mutation abolishes the interaction of Eap1p with eIF4E. Eap1p competes with eIF4G (the large subunit of the cap-binding complex, eIF4F) and p20 for binding to eIF4E in vivo and inhibits cap-dependent translation in vitro. Targeted disruption of the EAP1 gene results in a temperature-sensitive phenotype and also confers partial resistance to growth inhibition by rapamycin. These data indicate that Eap1p plays a role in cell growth and implicates this protein in the TOR signaling cascade of S. cerevisiae.

Indexed as

Amino Acid SequenceAntifungal AgentsBinding, CompetitiveDrug Resistance, MicrobialEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GFungal ProteinsMolecular Sequence DataMutationPeptide Initiation FactorsPhosphoproteinsProtein BiosynthesisRNA CapsSaccharomyces cerevisiaeSignal TransductionSirolimusAntifungal AgentseIF4E-associated protein Eap1Eukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GFungal ProteinsPeptide Initiation FactorsPhosphoproteinsRNA CapsSirolimus

Identifiers

PMID10848587
PMCPMC85860
OpenAlexW2100428689

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.