Evidence map›Paper›PMID 21764780›Full record

ArticleNucleic acids research2011

A novel 4E-interacting protein in Leishmania is involved in stage-specific translation pathways.

Alexandra Zinoviev, Mélissa Léger, Gerhard Wagner, Michal Shapira

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. 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
2.4field-weighted citation impact, top 12% 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, 79 citations in OpenAlex.

  1. Article
  2. Structural basis of secreted acid phosphatase polymerization in the Leishmania parasite.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. LeishIF3d is a non-canonical cap-binding protein inFrontiers in molecular biosciences · 2023
    Article
  10. Article
  11. Promastigote-to-Amastigote Conversion inPathogens (Basel, Switzerland) · 2022
    Review
  12. Article
  13. Article
  14. Characterization of an Atypical eIF4E Ortholog inInternational journal of molecular sciences · 2021
    Article
  15. Article
  16. LeishIF4E-5 Is a Promastigote-Specific Cap-Binding Protein inInternational journal of molecular sciences · 2021
    Article
  17. Article
  18. Review
  19. TheGenes · 2021
    Article
  20. 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

4 authors at 2 institutions in 2 countries.

Alexandra ZinovievDepartment of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva 84105, Israel.
Mélissa Léger
Gerhard Wagner
Michal Shapira
Ben-Gurion University of the Negev · ILHarvard University · US

Funding

STRUCTURAL BASIS OF TRANSLATION INITIATION BY EIF-4ER01CA068262 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1996 to 2015
$3.6M
NCI NIH HHS CA068262NCI NIH HHS R01 CA068262
6 · The paper itself

Abstract

In eukaryotes, exposure to stress conditions causes a shift from cap-dependent to cap-independent translation. In trypanosomatids, environmental switches are the driving force of a developmental program of gene expression, but it is yet unclear how their translation machinery copes with their constantly changing environment. Trypanosomatids have a unique cap structure (cap-4) and encode four highly diverged paralogs of the cap-binding protein, eIF4E; none were found to genetically complement a yeast mutant failing to express eIF4E. Here we show that in promastigotes, a typical cap-binding complex is anchored through LeishIF4E-4, which associates with components of the cap-binding pre-initiation complex. In axenic amastigotes, expression of LeishIF4E-4 decreases and the protein does not bind the cap, whereas LeishIF4E-1 maintains its expression level and associates with the cap structure and with translation initiation factors. However, LeishIF4E-1 does not interact with eIF4G-like proteins in both life stages, excluding its involvement in cap-dependent translation. Using pull-down assays and mass-spectrometry, we identified a novel, non-conserved 4E-Interacting Protein (Leish4E-IP), which binds to LeishIF4E-1 in promastigotes, but not in amastigotes. Yeast two-hybrid and NMR spectroscopy confirmed the specificity of this interaction. We propose that Leish4E-IP is a translation regulator that is involved in switching between cap-dependent and alternative translation pathways.

Indexed as

Peptide Chain Initiation, TranslationalEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4FEukaryotic Initiation FactorsLeishmaniaProtozoan ProteinsEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4FEukaryotic Initiation FactorsProtozoan Proteins

Identifiers

PMID21764780
PMCPMC3201875
OpenAlexW2057717261

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.