Evidence map›Paper›PMID 27807005›Full record

ArticleJournal of cell science2016

Inappropriate expression of the translation elongation factor 1A disrupts genome stability and metabolism.

Daniel J Tarrant, Mariarita Stirpe, Michelle Rowe, Mark J Howard, Tobias von der Haar, Campbell W Gourlay

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Autism- and epilepsy-associatedProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. 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

6 authors at 2 institutions in 2 countries.

Daniel J TarrantKent Fungal Group, School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK.
Mariarita StirpeDepartment of Biology and Biotechnology, Sapienza, University of Rome, 00185 Rome, Italy.
Michelle RoweKent Fungal Group, School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK.
Mark J HowardKent Fungal Group, School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK.
Tobias von der HaarKent Fungal Group, School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK tv@kent.ac.uk C.W.Gourlay@kent.ac.uk.ORCID 0000-0002-6031-9254
Campbell W GourlayKent Fungal Group, School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK tv@kent.ac.uk C.W.Gourlay@kent.ac.uk.ORCID 0000-0002-2373-6788
University of Kent · GBSapienza University of Rome · IT

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council 78573
6 · The paper itself

Abstract

The translation elongation factor eEF1A is one of the most abundant proteins found within cells, and its role within protein synthesis is well documented. Levels of eEF1A are tightly controlled, with inappropriate expression linked to oncogenesis. However, the mechanisms by which increased eEF1A expression alters cell behaviour are unknown. Our analyses in yeast suggest that elevation of eEF1A levels leads to stabilisation of the spindle pole body and changes in nuclear organisation. Elevation of the eEF1A2 isoform also leads to altered nuclear morphology in cultured human cells, suggesting a conserved role in maintaining genome stability. Gene expression and metabolomic analyses reveal that the level of eEF1A is crucial for the maintenance of metabolism and amino acid levels in yeast, most likely because of its role in the control of vacuole function. Increased eEF1A2 levels trigger lysosome biogenesis in cultured human cells, also suggesting a conserved role within metabolic control mechanisms. Taken together, our data suggest that the control of eEF1A levels is important for the maintenance of a number of cell functions beyond translation and that its de-regulation might contribute to its oncogenic properties.

Indexed as

Amino AcidsCarbonCell NucleusDynactin ComplexGenomic InstabilityHEK293 CellsHomeostasisHumansSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpindle ApparatusVacuolesAmino AcidsCarbonDynactin ComplexSaccharomyces cerevisiae ProteinsActin cytoskeletonAmino acid regulationeEF1AOncogeneSpindle pole bodyTrehaloseVacuole, Genome stability

Identifiers

PMID27807005
PMCPMC5201016
OpenAlexW2547407364

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.