Evidence map›Paper›PMID 23584478›Full record

ArticleOncogene2014

Glycogen synthase kinase-3β positively regulates protein synthesis and cell proliferation through the regulation of translation initiation factor 4E-binding protein 1.

S Shin, L Wolgamott, J Tcherkezian, S Vallabhapurapu, Y Yu, P P Roux, S-O Yoon

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

65 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. IBtkα Activates the β-Catenin-Dependent Transcription ofInternational journal of molecular sciences · 2022
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Berberine RepressesMolecular pharmacology · 2021
    Article
  20. Article

5 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

7 authors at 2 institutions in 1 country.

S ShinDepartment of Cancer and Cell Biology, University of Cincinnati College of Medicine, Cincinnati, OH, USA.
L WolgamottDepartment of Cancer and Cell Biology, University of Cincinnati College of Medicine, Cincinnati, OH, USA.
J TcherkezianDepartment of Pathology and Cell Biology, Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, Quebec, Canada.
S VallabhapurapuDepartment of Cancer and Cell Biology, University of Cincinnati College of Medicine, Cincinnati, OH, USA.
Y YuDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX, USA.
P P RouxDepartment of Pathology and Cell Biology, Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, Quebec, Canada.
S-O YoonDepartment of Cancer and Cell Biology, University of Cincinnati College of Medicine, Cincinnati, OH, USA.
University of Cincinnati Medical Center · USThe University of Texas Southwestern Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein synthesis has a key role in the control of cell proliferation, and its deregulation is associated with pathological conditions, notably cancer. Rapamycin, an inhibitor of mammalian target of rapamycin complex 1 (mTORC1), was known to inhibit protein synthesis. However, it does not substantially inhibit protein synthesis and cell proliferation in many cancer types. We were interested in finding a novel target in rapamycin-resistant cancer. The rate-limiting factor for translation is eukaryotic translation initiation factor 4E (eIF4E), which is negatively regulated by eIF4E-binding protein 1 (4E-BP1). Here, we provide evidence that glycogen synthase kinase (GSK)-3β promotes cell proliferation through positive regulation of protein synthesis. We found that GSK-3β phosphorylates and inactivates 4E-BP1, thereby increasing eIF4E-dependent protein synthesis. Considering the clinical relevance of pathways regulating protein synthesis, our study provides a promising new strategy and target for cancer therapy.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCell Cycle ProteinsCell Growth ProcessesEnzyme InhibitorsFemaleGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHumansMiceMice, NudePeptide Initiation FactorsPhosphoproteinsPhosphorylationProtein BindingProtein BiosynthesisAdaptor Proteins, Signal TransducingCell Cycle ProteinsEIF4EBP1 protein, humanEnzyme InhibitorsGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaGSK3B protein, humanGsk3b protein, mouseN-(4-methoxybenzyl)-N'-(5-nitro-1,3-thiazol-2-yl)ureaPeptide Initiation FactorsPhosphoproteinsThiazolesUrea

Identifiers

PMID23584478
OpenAlexW2000324903

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.