Evidence map›Paper›PMID 15961545›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Fibronectin controls cap-dependent translation through beta1 integrin and eukaryotic initiation factors 4 and 2 coordinated pathways.

Chiara Gorrini, Fabrizio Loreni, Valentina Gandin, Leonardo A Sala, Nahum Sonenberg, Pier Carlo Marchisio, Stefano Biffo

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

20 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Phosphorylation of Arl4A/D promotes their binding by the HYPK chaperone for their stable recruitment to the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Intracellular mRNA transport and localized translation.Nature reviews. Molecular cell biology · 2021
    Review
  7. Integrin β6 can be translationally regulated by eukaryotic initiation factor 4E: Contributing to colonic tumor malignancy.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Article
  8. Radiation Enhancement of Head and Neck Squamous Cell Carcinoma by the Dual PI3K/mTOR Inhibitor PF-05212384.Clinical cancer research : an official journal of the American Association for Cancer Research · 2015
    Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Extracellular matrix regulation of autophagy.Current opinion in cell biology · 2008
    Review
  19. Article
  20. Article
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.

Chiara GorriniMolecular Histology Unit, San Raffaele Institute, 20132 Milan, Italy.
Fabrizio Loreni
Valentina Gandin
Leonardo A Sala
Nahum Sonenberg
Pier Carlo Marchisio
Stefano Biffo
Università degli Studi del Piemonte Orientale “Amedeo Avogadro” · ITVita-Salute San Raffaele University · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fibronectin (FN) is a major matrix protein involved in multiple processes. Little is known about how adhesion to FN affects the translational machinery. We show that in fibroblasts adhesion to FN triggers translation through the coordinated regulation of eukaryotic initiation factors (eIFs) 4F and 2 and is impaired by blocking beta1 integrin engagement. FN-stimulated translation has unique properties: (i) it is highly sensitive to the inhibition of phosphatidylinositol 3-kinase (PI3K), but not to the inhibition of mammalian target of rapamycin, downstream of PI3K; (ii) there is no synergy between serum-stimulated translation and FN-dependent translation; (iii) FN-dependent translation, unlike growth factor-stimulated translation, does not lead to increased translocation of 5' terminal oligopyrimidine tract mRNAs to polysomes; and (iv) cells devoid of attachment to matrix show an impairment of initiation of translation accompanied by phosphorylation of eIF2alpha, which cannot be reverted by active PI3K. These findings indicate that integrins may recruit the translational machinery in a unique way and that FN-dependent translation cannot be blocked by mammalian target of rapamycin inhibition.

Indexed as

Protein BiosynthesisAnimalsBlotting, NorthernCell AdhesionCell LineEnzyme InhibitorsEukaryotic Initiation Factor-2FibroblastsFibronectinsGuanosine TriphosphateHumansImmunoblottingIntegrin beta1IntegrinsMiceNIH 3T3 CellseIF-4Enzyme InhibitorsEukaryotic Initiation Factor-2FibronectinsGuanosine TriphosphateIntegrin beta1IntegrinsMTOR protein, humanmTOR protein, mousePeptide Initiation FactorsPhosphatidylinositol 3-KinasesProtein KinasesProteinsPyrimidinesRNARNA, MessengerTOR Serine-Threonine Kinases

Identifiers

PMID15961545
PMCPMC1166589
OpenAlexW2077474908

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.