Evidence map›Paper›PMID 14982957›Full record

ArticleNucleic acids research2004

The active form of Xp54 RNA helicase in translational repression is an RNA-mediated oligomer.

Nicola Minshall, Nancy Standart

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

54 citing papers in PubMed, 121 citations in OpenAlex.

  1. Med9 Is a Novel eIF4E-Interacting Protein inInternational journal of molecular sciences · 2026
    Article
  2. Role of DEAD/DEAH-box helicases in immunity, infection and cancers.Cell communication and signaling : CCS · 2025
    Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Numerous interactions act redundantly to assemble a tunable size of P bodies inProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Translational repression of theRNA (New York, N.Y.) · 2017
    Article
  10. Article
  11. Article
  12. Article
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  14. Article
  15. Article
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  17. Article
  18. Review
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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 1 institution in 1 country.

Nicola MinshallDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK.
Nancy Standart
University of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previously, we reported that in clam oocytes, cytoplasmic polyadenylation element-binding protein (CPEB) co-immunoprecipitates with p47, a member of the highly conserved RCK family of RNA helicases which includes Drosophila Me31B and Saccharomyces cerevisiae Dhh1. Xp54, the Xenopus homologue, with helicase activity, is a component of stored mRNP. In tethered function assays in Xenopus oocytes, we showed that MS2-Xp54 represses the translation of non-adenylated firefly luciferase mRNAs and that mutations in two core helicase motifs, DEAD and HRIGR, surprisingly, activated translation. Here we show that wild-type MS2-Xp54 tethered to the reporter mRNA 3'-untranslated region (UTR) represses translation in both oocytes and eggs in an RNA-dependent complex with endogenous Xp54. Injection of mutant helicases or adenylated reporter mRNA abrogates this association. Thus Xp54 oligomerization is a hallmark of translational repression. Xp54 complexes, which also contain CPEB and eIF4E in oocytes, change during meiotic maturation. In eggs, CPEB is degraded and, while eIF4E still interacts with Xp54, this interaction becomes RNA dependent. Supporting evidence for RNA-mediated oligomerization of endogenous Xp54, and RNA-independent association with CPEB and eIF4E in oocytes was obtained by gel filtration. Altogether, our data are consistent with a model in which the active form of the Xp54 RNA helicase is an oligomer in vivo which, when tethered, via either MS2 or CPEB to the 3'UTR, represses mRNA translation, possibly by sequestering eIF4E from the translational machinery.

Indexed as

Protein BiosynthesisAnimalsDEAD-box RNA HelicasesEukaryotic Initiation Factor-4EGene Expression RegulationMacromolecular SubstancesMeiosisModels, GeneticmRNA Cleavage and Polyadenylation FactorsMutationOocytesOvumRNA HelicasesRNA, MessengerTranscription FactorsXenopusCpeb1 protein, XenopusDEAD-box RNA HelicasesEukaryotic Initiation Factor-4EMacromolecular SubstancesmRNA Cleavage and Polyadenylation FactorsRNA HelicasesRNA, MessengerTranscription FactorsXenopus ProteinsXp54 RNA helicase, Xenopus

Identifiers

PMID14982957
PMCPMC390291
OpenAlexW2005826932

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.