Evidence map›Paper›PMID 19078965›Full record

ArticleThe EMBO journal2009

General RNA-binding proteins have a function in poly(A)-binding protein-dependent translation.

Yuri V Svitkin, Valentina M Evdokimova, Ann Brasey, Tatyana V Pestova, Daniel Fantus, Akiko Yanagiya, Hiroaki Imataka, Maxim A Skabkin, Lev P Ovchinnikov, William C Merrick and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

43 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Lighting up single-mRNA translation dynamics in living cells.Current opinion in genetics & development · 2020
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Cold Shock Proteins Mediate GN with Mesangioproliferation.Journal of the American Society of Nephrology : JASN · 2016
    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

11 authors at 6 institutions in 4 countries.

Yuri V SvitkinDepartment of Biochemistry and Goodman Cancer Center, McGill University, Montreal, Quebec, Canada.
Valentina M Evdokimova
Ann Brasey
Tatyana V Pestova
Daniel Fantus
Akiko Yanagiya
Hiroaki Imataka
Maxim A Skabkin
Lev P Ovchinnikov
William C Merrick
Nahum Sonenberg
McGill University · CAInstitute of Protein Research · RUCase Western Reserve University · USChildren’s Health Research Institute · CASUNY Downstate Health Sciences University · USSystems Biology Institute · JP

Funding

MECHANISM OF PROTEIN SYNTHESIS INTITIATIONR01GM026796 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI MERRICK, WILLIAM C. · 1985 to 2008
$2.6M
Translational control by poly(A)-binding protein and its modulators (Paips)R01GM066157 · NIGMS · MCGILL UNIVERSITY · PI SONENBERG, NAHUM · 2002 to 2011
$1.6M
NIGMS NIH HHS GM26796NIGMS NIH HHS GM66157NIGMS NIH HHS R01 GM026796NIGMS NIH HHS R01 GM066157
6 · The paper itself

Abstract

The interaction between the poly(A)-binding protein (PABP) and eukaryotic translational initiation factor 4G (eIF4G), which brings about circularization of the mRNA, stimulates translation. General RNA-binding proteins affect translation, but their role in mRNA circularization has not been studied before. Here, we demonstrate that the major mRNA ribonucleoprotein YB-1 has a pivotal function in the regulation of eIF4F activity by PABP. In cell extracts, the addition of YB-1 exacerbated the inhibition of 80S ribosome initiation complex formation by PABP depletion. Rabbit reticulocyte lysate in which PABP weakly stimulates translation is rendered PABP-dependent after the addition of YB-1. In this system, eIF4E binding to the cap structure is inhibited by YB-1 and stimulated by a nonspecific RNA. Significantly, adding PABP back to the depleted lysate stimulated eIF4E binding to the cap structure more potently if this binding had been downregulated by YB-1. Conversely, adding nonspecific RNA abrogated PABP stimulation of eIF4E binding. These data strongly suggest that competition between YB-1 and eIF4G for mRNA binding is required for efficient stimulation of eIF4F activity by PABP.

Indexed as

Protein BiosynthesisAnimalsCell ExtractsCell LineDNA-Binding ProteinsEukaryotic Initiation Factor-4FMiceModels, BiologicalNuclear ProteinsPoly(A)-Binding ProteinsRabbitsY-Box-Binding Protein 1Cell ExtractsDNA-Binding ProteinsEukaryotic Initiation Factor-4FNuclear ProteinsPoly(A)-Binding ProteinsY-Box-Binding Protein 1YBX1 protein, human

Identifiers

PMID19078965
PMCPMC2633083
OpenAlexW2127315544

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.