Evidence map›Paper›PMID 24923804›Full record

ArticleGenetics2014

Fertility and polarized cell growth depends on eIF5A for translation of polyproline-rich formins in Saccharomyces cerevisiae.

Tianlu Li, Borja Belda-Palazón, Alejandro Ferrando, Paula Alepuz

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. eIF5A coordinates the transcription and translation of its target genes.Cellular and molecular life sciences : CMLS · 2026
    Article
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  5. Article
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  7. Role of eIF5A in Mitochondrial Function.International journal of molecular sciences · 2022
    Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Translation Elongation and Recoding in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. 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 3 institutions in 1 country.

Tianlu LiDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universitat de València, E-46100 Burjassot, Valencia, Spain.
Borja Belda-PalazónInstituto de Biología Molecular y Celular de Plantas, Centro Superior de Investigaciones Científicas-Universidad Politécnica de Valencia, 46022 Valencia, Spain.
Alejandro FerrandoInstituto de Biología Molecular y Celular de Plantas, Centro Superior de Investigaciones Científicas-Universidad Politécnica de Valencia, 46022 Valencia, Spain paula.alepuz@uv.es aferrando@ibmcp.upv.es.
Paula AlepuzDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universitat de València, E-46100 Burjassot, Valencia, Spain paula.alepuz@uv.es aferrando@ibmcp.upv.es.
Universitat de València · ESInstituto de Biología Molecular y Celular de Plantas · ESUniversitat Politècnica de València · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

eIF5A is an essential and evolutionary conserved translation elongation factor, which has recently been proposed to be required for the translation of proteins with consecutive prolines. The binding of eIF5A to ribosomes occurs upon its activation by hypusination, a modification that requires spermidine, an essential factor for mammalian fertility that also promotes yeast mating. We show that in response to pheromone, hypusinated eIF5A is required for shmoo formation, localization of polarisome components, induction of cell fusion proteins, and actin assembly in yeast. We also show that eIF5A is required for the translation of Bni1, a proline-rich formin involved in polarized growth during shmoo formation. Our data indicate that translation of the polyproline motifs in Bni1 is eIF5A dependent and this translation dependency is lost upon deletion of the polyprolines. Moreover, an exogenous increase in Bni1 protein levels partially restores the defect in shmoo formation seen in eIF5A mutants. Overall, our results identify eIF5A as a novel and essential regulator of yeast mating through formin translation. Since eIF5A and polyproline formins are conserved across species, our results also suggest that eIF5A-dependent translation of formins could regulate polarized growth in such processes as fertility and cancer in higher eukaryotes.

Indexed as

Peptide Chain Elongation, TranslationalActinsCytoskeletal ProteinsEukaryotic Translation Initiation Factor 5AMembrane ProteinsMicrofilament ProteinsMorphogenesisMutationPeptide Initiation FactorsPeptidesProtein Structure, TertiaryQc-SNARE ProteinsRibosomesRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsBni1 protein, S cerevisiaeCytoskeletal ProteinsEukaryotic Translation Initiation Factor 5AFUS1 protein, S cerevisiaeMembrane ProteinsMicrofilament ProteinsPeptide Initiation FactorsPeptidespolyprolineQc-SNARE ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSPA2 protein, S cerevisiaeUse1 protein, S cerevisiaeeIF5Aforminsmatingpolarized growthtranslation

Identifiers

PMID24923804
PMCPMC4125393
OpenAlexW2135786108

What Socratic 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 Socratic graph.