Evidence map›Paper›PMID 33460649›Full record

ArticleThe Journal of biological chemistry

Medulloblastoma-associated mutations in the DEAD-box RNA helicase DDX3X/DED1 cause specific defects in translation.

Nicolette P Brown, Ashley M Vergara, Alisha B Whelan, Paolo Guerra, Timothy A Bolger

Abstract read
In one paragraph

Article in The Journal of biological chemistry. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. The human DEAD-box helicase DDX3X as a regulator of mRNA translation.Frontiers in cell and developmental biology · 2022
    Review
  12. Article
  13. RNA-binding proteins of COSMIC importance in cancer.The Journal of clinical investigation · 2021
    Review
  14. Article
  15. 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

5 authors.

Nicolette P BrownDepartment of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona, USA.
Ashley M VergaraDepartment of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona, USA.
Alisha B WhelanDepartment of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona, USA.
Paolo GuerraDepartment of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona, USA.
Timothy A BolgerDepartment of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona, USA. Electronic address: tbolger@arizona.edu.

Funding

Regulation of the Translational Response to Cellular StressR01GM136827 · NIGMS · UNIVERSITY OF GEORGIA · PI BOLGER, TIMOTHY A · 2020 to 2024
$1.5M
NIGMS NIH HHS R01 GM136827
6 · The paper itself

Abstract

Medulloblastoma is the most common pediatric brain cancer, and sequencing studies identified frequent mutations in DDX3X, a DEAD-box RNA helicase primarily implicated in translation. Forty-two different sites were identified, suggesting that the functional effects of the mutations are complex. To investigate how these mutations are affecting DDX3X cellular function, we constructed a full set of equivalent mutant alleles in DED1, the Saccharomyces cerevisiae ortholog of DDX3X, and characterized their effects in vivo and in vitro. Most of the medulloblastoma-associated mutants in DDX3X/DED1 (ded1-mam) showed substantial growth defects, indicating that functional effects are conserved in yeast. Further, while translation was affected in some mutants, translation defects affecting bulk mRNA were neither consistent nor correlated with the growth phenotypes. Likewise, increased formation of stress granules in ded1-mam mutants was common but did not correspond to the severity of the mutants' growth defects. In contrast, defects in translating mRNAs containing secondary structure in their 5' untranslated regions (UTRs) were found in almost all ded1-mam mutants and correlated well with growth phenotypes. We thus conclude that these specific translation defects, rather than generalized effects on translation, are responsible for the observed cellular phenotypes and likely contribute to DDX3X-mutant medulloblastoma. Examination of ATPase activity and RNA binding of recombinant mutant proteins also did not reveal a consistent defect, indicating that the translation defects are derived from multiple enzymatic deficiencies. This work suggests that future studies into medulloblastoma pathology should focus on this specific translation defect, while taking into account the wide spectrum of DDX3X mutations.

Indexed as

Protein Biosynthesis5' Untranslated RegionsAdenosine TriphosphatasesAmino Acid SubstitutionCerebellar NeoplasmsConserved SequenceDEAD-box RNA HelicasesGenes, ReporterGreen Fluorescent ProteinsHumansLuminescent ProteinsMedulloblastomaMutagenesis, Site-DirectedMutationPhenotypeProtein Binding5' Untranslated RegionsAdenosine TriphosphatasesDDX3X protein, humanDEAD-box RNA HelicasesDED1 protein, S cerevisiaeGreen Fluorescent ProteinsLuminescent ProteinsRecombinant ProteinsRed Fluorescent ProteinRNASaccharomyces cerevisiae ProteinscancerDEAD-box proteinmedulloblastomaRNA helicaseSaccharomyces cerevisiaestart site scanningstress granuletranslation initiationtranslation regulation

Identifiers

PMID33460649
PMCPMC7949108

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Registered trials

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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.