Evidence map›Paper›PMID 24644291›Full record

ArticleThe Journal of biological chemistry2014

Musashi protein-directed translational activation of target mRNAs is mediated by the poly(A) polymerase, germ line development defective-2.

Chad Cragle, Angus M MacNicol

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

38 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Isoform-Specific Localization Diversifies Human MSI2 Function.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. RNA-Binding Proteins: Modulators of Canonical Wnt Signaling Pathway.International journal of molecular sciences · 2025
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Msi2-mediated MiR7a-1 processing repression promotes myogenesis.Journal of cachexia, sarcopenia and muscle · 2022
    Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Auto-regulatory feedback by RNA-binding proteins.Journal of molecular cell biology · 2019
    Review
  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

2 authors at 2 institutions in 1 country.

Chad CragleFrom the Interdiciplinary Biomedical Sciences, Departments of Neurobiology and Developmental Sciences.
Angus M MacNicolDepartments of Neurobiology and Developmental Sciences, Physiology and Biophysics, and Genetics, Winthrop P. Rockefeller Cancer Institute, University of Arkansas for Medical Sciences, Little Rock, Arkansas 722205 Angus@UAMS.edu.
University of Arkansas for Medical Sciences · USWinthrop Rockefeller Foundation · US

Funding

Arkansas Center for Clinical and Translational ResearchUL1TR000039 · NCATS · UNIV OF ARKANSAS FOR MED SCIS · PI BECK, CORNELIA MARIE, JAMES, LAURA P · 2012 to 2014
$10.0M
Maternal gene regulation in early veterbrate developmentR01HD035688 · NICHD · UNIV OF ARKANSAS FOR MED SCIS · PI MACNICOL, ANGUS M · 1999 to 2011
$2.5M
Arkansas Center for Clinical Translational ResearchKL2TR000063 · NCATS · UNIV OF ARKANSAS FOR MED SCIS · PI BECK, CORNELIA MARIE, JAMES, LAURA P · 2012 to 2014
$459k
NCATS NIH HHS KL2 TR000063NCATS NIH HHS KL2TR000063NCATS NIH HHS UL1 TR000039NCATS NIH HHS UL1TR000039NICHD NIH HHS R01 HD035688NICHD NIH HHS R01 HD35688
6 · The paper itself

Abstract

The mRNA-binding protein, Musashi, has been shown to regulate translation of select mRNAs and to control cellular identity in both stem cells and cancer cells. Within the mammalian cells, Musashi has traditionally been characterized as a repressor of translation. However, we have demonstrated that Musashi is an activator of translation in progesterone-stimulated oocytes of the frog Xenopus laevis, and recent evidence has revealed Musashi's capability to function as an activator of translation in mammalian systems. The molecular mechanism by which Musashi directs activation of target mRNAs has not been elucidated. Here, we report a specific association of Musashi with the noncanonical poly(A) polymerase germ line development defective-2 (GLD2) and map the association domain to 31 amino acids within the C-terminal domain of Musashi. We show that loss of GLD2 interaction through deletion of the binding domain or treatment with antisense oligonucleotides compromises Musashi function. Additionally, we demonstrate that overexpression of both Musashi and GLD2 significantly enhances Musashi function. Finally, we report a similar co-association also occurs between murine Musashi and GLD2 orthologs, suggesting that coupling of Musashi to the polyadenylation apparatus is a conserved mechanism to promote target mRNA translation.

Indexed as

Gene Expression RegulationProtein BiosynthesisAnimalsCell CycleCytoplasmMiceNerve Tissue ProteinsPolyadenylationPolynucleotide AdenylyltransferaseRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerSubstrate SpecificityXenopus laevisXenopus ProteinsMsi1 protein, XenopusNerve Tissue ProteinsPolynucleotide AdenylyltransferaseRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerTENT2 protein, XenopusXenopus ProteinsOocytePolyadenylationRNA-binding ProteinTranslation ControlXenopus

Identifiers

PMID24644291
PMCPMC4022889
OpenAlexW2035905798

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.