Evidence map›Paper›PMID 16354698›Full record

ArticleMolecular and cellular biology2006

Akt-mediated YB-1 phosphorylation activates translation of silent mRNA species.

Valentina Evdokimova, Peter Ruzanov, Michael S Anglesio, Alexey V Sorokin, Lev P Ovchinnikov, Jonathan Buckley, Timothy J Triche, Nahum Sonenberg, Poul H B Sorensen

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

132 citing papers in PubMed, 257 citations in OpenAlex.

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  7. The Impact of Pdcd4, a Translation Inhibitor, on Drug Resistance.Pharmaceuticals (Basel, Switzerland) · 2024
    Review
  8. Article
  9. YB-1 activating cascades as potential targets in KRAS-mutated tumors.Strahlentherapie und Onkologie : Organ der Deutschen Rontgengesellschaft ... [et al] · 2023
    Review
  10. Review
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  18. YB-1 Phosphorylation at Serine 209 Inhibits Its Nuclear Translocation.International journal of molecular sciences · 2021
    Article
  19. Article
  20. Article

72 more citing papers are in PubMed but not listed here.

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

9 authors at 5 institutions in 3 countries.

Valentina EvdokimovaDepartment of Pathology, British Columbia Research Institute for Children's and Women's Health, Vancouver, BC, Canada V5Z 163. evdokimo@interchange.ubc.ca
Peter Ruzanov
Michael S Anglesio
Alexey V Sorokin
Lev P Ovchinnikov
Jonathan Buckley
Timothy J Triche
Nahum Sonenberg
Poul H B Sorensen
Children's Hospital of Los Angeles · USInstitute of Protein Research · RUGenome British Columbia · CAMcGill University · CAUniversity of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

YB-1 is a broad-specificity RNA-binding protein that is involved in regulation of mRNA transcription, splicing, translation, and stability. In both germinal and somatic cells, YB-1 and related proteins are major components of translationally inactive messenger ribonucleoprotein particles (mRNPs) and are mainly responsible for storage of mRNAs in a silent state. However, mechanisms regulating the repressor activity of YB-1 are not well understood. Here we demonstrate that association of YB-1 with the capped 5' terminus of the mRNA is regulated via phosphorylation by the serine/threonine protein kinase Akt. In contrast to its nonphosphorylated form, phosphorylated YB-1 fails to inhibit cap-dependent but not internal ribosome entry site-dependent translation of a reporter mRNA in vitro. We also show that similar to YB-1, Akt is associated with inactive mRNPs and that activated Akt may relieve translational repression of the YB-1-bound mRNAs. Using Affymetrix microarrays, we found that many of the YB-1-associated messages encode stress- and growth-related proteins, raising the intriguing possibility that Akt-mediated YB-1 phosphorylation could, in part, increase production of proteins regulating cell proliferation, oncogenic transformation, and stress response.

Indexed as

AnimalsGene Expression RegulationGene SilencingHumansMiceNIH 3T3 CellsOligonucleotide Array Sequence AnalysisPhosphorylationProtein BiosynthesisProto-Oncogene Proteins c-aktRibonucleoproteinsRNA Cap-Binding ProteinsRNA CapsRNA, MessengerY-Box-Binding Protein 1messenger ribonucleoproteinProto-Oncogene Proteins c-aktRibonucleoproteinsRNA Cap-Binding ProteinsRNA CapsRNA, MessengerY-Box-Binding Protein 1

Identifiers

PMID16354698
PMCPMC1317623
OpenAlexW2107318020

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.