Evidence map›Paper›PMID 12490714›Full record

ArticleNucleic acids research2002

Identification of cellular mRNA targets for RNA-binding protein Sam68.

Michiyasu Itoh, Izumi Haga, Qing-Hua Li, Jun-ichi Fujisawa

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

36 citing papers in PubMed, 68 citations in OpenAlex.

  1. RNA-binding proteins in bone pathophysiology.Frontiers in cell and developmental biology · 2024
    Review
  2. Article
  3. Article
  4. Review
  5. β-Actin mRNA interactome mapping by proximity biotinylation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  6. Article
  7. Review
  8. Imaging mRNA and protein interactions within neurons.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Article
  10. Review
  11. Article
  12. Impacts of Alternative Splicing Events on the Differentiation of Adipocytes.International journal of molecular sciences · 2015
    Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Role of Sam68 in post-transcriptional gene regulation.International journal of molecular sciences · 2013
    Review
  19. RNA-binding protein Sam68 controls synapse number and local β-actin mRNA metabolism in dendrites.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

4 authors at 1 institution in 1 country.

Michiyasu ItohDepartment of Microbiology, Kansai Medical University, 10-15 Fumizono-cho, Moriguchi, Osaka 570-8506, Japan.
Izumi Haga
Qing-Hua Li
Jun-ichi Fujisawa
Kansai Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sam68 (Src-associated in mitosis, 68 kDa), a nuclear RNA-binding protein, has been postulated to play a role in cell-growth control as a modulator of signal transduction and activation of RNA metabolism. Although Sam68 was demonstrated to bind to the UAAA sequences in synthetic oligoribonucleotides and poly(U) homopolymers in vitro, the legitimate cellular mRNA target remained unclear. By using the differential display and cDNA-representational difference analysis techniques, followed by reverse transcription polymerase chain reaction of RNAs co-immunoprecipitated with Sam68 from a HeLa cell lysate, we identified 10 mRNA species that bind in vivo to Sam68 in an RNA-binding domain-dependent manner. Among them, the mRNA species for hnRNP A2/B1 and beta-actin were found to bind prominently in vivo as well as in vitro, suggesting the possible involvement of Sam68 in the post- transcriptional regulation of these genes. Mapping of the Sam68-binding sequence revealed that Sam68 associates with these mRNAs through different nucleotide motifs, UAAA for hnRNP A2/B1 mRNA and UUUUUU for beta-actin mRNA, and that both binding sequences must reside in a loop structure for recognition by Sam68. The results indicated that Sam68 recognizes both the UAAA motif and poly(U) sequences in vivo for binding to cellular target mRNAs.

Indexed as

3' Untranslated RegionsActinsAdaptor Proteins, Signal TransducingBase SequenceBinding SitesDNA-Binding ProteinsDNA, ComplementaryGlutathione TransferaseHeLa CellsHeterogeneous-Nuclear RibonucleoproteinsHumansMolecular Sequence DataMutationNucleic Acid ConformationProtein BindingRecombinant Fusion Proteins3' Untranslated RegionsActinsAdaptor Proteins, Signal TransducingDNA-Binding ProteinsDNA, ComplementaryGlutathione TransferaseHeterogeneous-Nuclear RibonucleoproteinsKHDRBS1 protein, humanRecombinant Fusion ProteinsRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID12490714
PMCPMC140046
OpenAlexW1997623360

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.