Evidence map›Paper›PMID 18711726›Full record

ArticleJournal of neuroscience research2009

Specific interaction between Sam68 and neuronal mRNAs: implication for the activity-dependent biosynthesis of elongation factor eEF1A.

Julien Grange, Agnès Belly, Stéphane Dupas, Alain Trembleau, Rémy Sadoul, Yves Goldberg

Open access · greenAbstract read
In one paragraph

Article in Journal of neuroscience research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Regionally restricted modulation ofFrontiers in molecular neuroscience · 2022
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. RNA-binding protein Sam68 controls synapse number and local β-actin mRNA metabolism in dendrites.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  9. Article
  10. Review
  11. Orphan nuclear bodies.Cold Spring Harbor perspectives in biology · 2010
    Review
  12. Article
  13. Article
  14. Article
  15. 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 4 institutions in 2 countries.

Julien GrangeUniversité Joseph Fourier, Grenoble Institute of Neuroscience, Grenoble, France.
Agnès Belly
Stéphane Dupas
Alain Trembleau
Rémy Sadoul
Yves Goldberg
Centre National de la Recherche Scientifique · FRInserm · FRUniversité Joseph Fourier · FRZero to Three · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In cultured hippocampal neurons and in adult brain, the splicing regulatory protein Sam68 is partially relocated to the somatodendritic domain and associates with dendritic polysomes. Transfer to the dendrites is activity-dependent. We have investigated the repertoire of neuronal mRNAs to which Sam68 binds in vivo. By using coimmunoprecipitation and microarray screening techniques, Sam68 was found to associate with a number of plasticity-related mRNA species, including Eef1a1, an activity-responsive mRNA coding for translation elongation factor eEF1A. In cortical neuronal cultures, translation of the Eef1a1 mRNA was strongly induced by neuronal depolarisation and correlated with enhanced association of Sam68 with polysomal mRNAs. The possible function of Sam68 in Eef1a1 mRNA utilization was studied by expressing a dominant-negative, cytoplasmic Sam68 mutant (GFP-Sam68DeltaC) in cultured hippocampal neurons. The level of eEF1A was lower in neurons expressing GFP-Sam68DeltaC than in control neurons, supporting the proposal that endogenous Sam68 may contribute to the translational efficiency of the Eef1a1 mRNA. These findings are discussed in the light of the complex, potentially crucial regulation of eEF1A biosynthesis during long-term synaptic change.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCells, CulturedDNA-Binding ProteinsEmbryo, MammalianGene Expression RegulationHippocampusHumansImmunoprecipitationNeuronsPeptide Elongation Factor 1Protein BindingProtein BiosynthesisRatsReceptors, N-Methyl-D-AspartateRNA-Binding ProteinsAdaptor Proteins, Signal TransducingDNA-Binding ProteinsKHDRBS1 protein, humanPeptide Elongation Factor 1Receptors, N-Methyl-D-AspartateRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID18711726
PMCPMC2840017
OpenAlexW2145301598

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.