Evidence map›Paper›PMID 19850929›Full record

ArticleThe Journal of biological chemistry2009

The Hsp90 inhibitor geldanamycin abrogates colocalization of eIF4E and eIF4E-transporter into stress granules and association of eIF4E with eIF4G.

Yukari Suzuki, Michiko Minami, Miho Suzuki, Keiko Abe, Shuhei Zenno, Masafumi Tsujimoto, Ken Matsumoto, Yasufumi Minami

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Heat shock proteins-driven stress granule dynamics: yet another avenue for cell survival.Apoptosis : an international journal on programmed cell death · 2021
    Review
  6. Article
  7. Lithium Chloride Sensitivity in Yeast and Regulation of Translation.International journal of molecular sciences · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Human RNAi pathway: crosstalk with organelles and cells.Functional & integrative genomics · 2014
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. The therapeutic target Hsp90 and cancer hallmarks.Current pharmaceutical design · 2013
    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

8 authors at 5 institutions in 1 country.

Yukari SuzukiGraduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Michiko Minami
Miho Suzuki
Keiko Abe
Shuhei Zenno
Masafumi Tsujimoto
Ken Matsumoto
Yasufumi Minami
Maebashi Institute of Technology · JPThe University of Tokyo · JPTokyo Gakugei University · JPJapan Science and Technology Agency · JPRIKEN Advanced Science Institute · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The eukaryotic translation initiation factor eIF4E plays a critical role in the control of translation initiation through binding to the mRNA 5' cap structure. eIF4E is also a component of processing bodies and stress granules, which are two types of cytoplasmic RNA granule in which translationally inactivated mRNAs accumulate. We found that treatment with the Hsp90 inhibitor geldanamycin leads to a substantial reduction in the number of HeLa cells that contain processing bodies. In contrast, stress granules are not disrupted but seem to be only partially affected by the inhibition of Hsp90. However, it is striking that eIF4E as well as its binding partner eIF4E transporter (4E-T), which mediates the import of eIF4E into the nucleus, are obviously lost from stress granules. Furthermore, the amount of eIF4G that is associated with the cap via eIF4E is reduced by geldanamycin treatment. Thus, the chaperone activity of Hsp90 probably contributes to the correct localization of eIF4E and 4E-T to stress granules and also to the interaction between eIF4E and eIF4G, both of which may be needed for eIF4E to acquire the physiological functionality that underlies the mechanism of translation initiation.

Indexed as

BenzoquinonesCytoplasmic GranulesEnzyme InhibitorsEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GHeLa CellsHSP90 Heat-Shock ProteinsHumansLactams, MacrocyclicNucleocytoplasmic Transport ProteinsPeptide Chain Initiation, TranslationalProtein TransportRNA CapsBenzoquinonesEIF4ENIF1 protein, humanEIF4G1 protein, humanEnzyme InhibitorsEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GgeldanamycinHSP90 Heat-Shock ProteinsLactams, MacrocyclicNucleocytoplasmic Transport ProteinsRNA Caps

Identifiers

PMID19850929
PMCPMC2790990
OpenAlexW2089426978

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.