Evidence map›Paper›PMID 25694449›Full record

ArticleMolecular biology of the cell2015

Cytoplasmic hGle1A regulates stress granules by modulation of translation.

Aditi, Andrew W Folkmann, Susan R Wente

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024
    Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. The human DEAD-box helicase DDX3X as a regulator of mRNA translation.Frontiers in cell and developmental biology · 2022
    Review
  10. Article
  11. Article
  12. Article
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  14. Article
  15. Article
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  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

3 authors at 1 institution in 1 country.

AditiDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
Andrew W FolkmannDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
Susan R WenteDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
Vanderbilt University · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
Integrated Biological Systems Training in OncologyT32CA119925 · NCI · VANDERBILT UNIVERSITY · PI Vivian Gama, William Patrick Tansey · 2008 to 2026
$7.6M
Molecular Analysis of Nuclear Pore Complex FunctionR37GM051219 · NIGMS · VANDERBILT UNIVERSITY · PI WENTE, SUSAN R. · 2010 to 2019
$5.6M
Defining the role for Gle1 in the fetal lethal motor neuron disease LCCS1F31NS070431 · NINDS · VANDERBILT UNIVERSITY · PI FOLKMANN, ANDREW WILLIAM · 2011 to 2013
$80k
NCI NIH HHS P30 CA068485NCI NIH HHS P30CA068485NCI NIH HHS T32 CA119925NIGMS NIH HHS 5R37GM051219NIGMS NIH HHS R37 GM051219NINDS NIH HHS F31 NS070431NINDS NIH HHS F31NS070431
6 · The paper itself

Abstract

When eukaryotic cells respond to stress, gene expression pathways change to selectively export and translate subsets of mRNAs. Translationally repressed mRNAs accumulate in cytoplasmic foci known as stress granules (SGs). SGs are in dynamic equilibrium with the translational machinery, but mechanisms controlling this are unclear. Gle1 is required for DEAD-box protein function during mRNA export and translation. We document that human Gle1 (hGle1) is a critical regulator of translation during stress. hGle1 is recruited to SGs, and hGLE1 small interfering RNA-mediated knockdown perturbs SG assembly, resulting in increased numbers of smaller SGs. The rate of SG disassembly is also delayed. Furthermore, SG hGle1-depletion defects correlate with translation perturbations, and the hGle1 role in SGs is independent of mRNA export. Interestingly, we observe isoform-specific roles for hGle1 in which SG function requires hGle1A, whereas mRNA export requires hGle1B. We find that the SG defects in hGle1-depleted cells are rescued by puromycin or DDX3 expression. Together with recent links of hGLE1 mutations in amyotrophic lateral sclerosis patients, these results uncover a paradigm for hGle1A modulating the balance between translation and SGs during stress and disease.

Indexed as

Stress, PhysiologicalCell LineCytoplasmic GranulesDown-RegulationHumansNucleocytoplasmic Transport ProteinsProtein BiosynthesisProtein IsoformsGle1 protein, humanNucleocytoplasmic Transport ProteinsProtein Isoforms

Identifiers

PMID25694449
PMCPMC4395128
OpenAlexW2110068937

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.