Evidence map›Paper›PMID 19762470›Full record

ArticleThe Journal of biological chemistry2009

Identification of a Sam68 ribonucleoprotein complex regulated by epidermal growth factor.

Marc-Etienne Huot, Gillian Vogel, Stéphane Richard

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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. RNA-binding proteins regulating the CD44 alternative splicing.Frontiers in molecular biosciences · 2023
    Review
  6. Article
  7. RNA-binding protein signaling in adult neurogenesis.Frontiers in cell and developmental biology · 2022
    Review
  8. Roles of Splicing Factors in Hormone-Related Cancer Progression.International journal of molecular sciences · 2020
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Role of Sam68 in post-transcriptional gene regulation.International journal of molecular sciences · 2013
    Review
  16. Review
  17. Article
  18. Article
  19. 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

3 authors at 1 institution in 1 country.

Marc-Etienne HuotTerry Fox Molecular Oncology Group and the Bloomfield Center for Research on Aging, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital, Montréal, Québec H3T 1E2, Canada.
Gillian Vogel
Stéphane Richard
McGill University · CA

Funding

Canadian Institutes of Health Research MT13377
6 · The paper itself

Abstract

Sam68, Src associated in mitosis of 68 kDa, is a known RNA-binding protein and a signaling adaptor protein for tyrosine kinases. However, the proteins associated with Sam68 and the existence of a Sam68 complex, its mass, and regulation are, however, unknown. Herein we identify a large Sam68 complex with a mass >1 MDa in HeLa cells that is composed of approximately 40 proteins using an immunoprecipitation followed by a mass spectrometry approach. Many of the proteins identified are RNA-binding proteins and are known components of a previously identified structure termed the spreading initiation center. The large Sam68 complex is a ribonucleoprotein complex, as treatment with RNases caused a shift in the molecular mass of the complex to 200-450 kDa. Moreover, treatment of HeLa cells with phorbol 12-myristate 13-acetate or epidermal growth factor induced the disassociation of Sam68 from the large complex and the appearance of Sam68 within the smaller complex. Actually, in certain cell lines such as breast cancer cell lines MCF-7 and BT-20, Sam68 exists in equilibrium between a large and a small complex. The appearance of the small Sam68 complex in cells correlates with the ability of Sam68 to promote the alternative splicing of CD44 and cell migration. Our findings show that Sam68 exists in equilibrium in transformed cells between two complexes and that extracellular signals, such as epidermal growth factor stimulation, promote alternative splicing by modulating the composition of the Sam68 complex.

Indexed as

Cell MovementAdaptor Proteins, Signal TransducingAlternative SplicingBlotting, WesternBreast NeoplasmsCell NucleusDNA-Binding ProteinsEpidermal Growth FactorFemaleFluorescent Antibody TechniqueHeLa CellsHumansHyaluronan ReceptorsImmunoprecipitationProtein BindingReverse Transcriptase Polymerase Chain ReactionAdaptor Proteins, Signal TransducingDNA-Binding ProteinsEpidermal Growth FactorHyaluronan ReceptorsKHDRBS1 protein, humanRNA-Binding ProteinsRNA, MessengerTetradecanoylphorbol Acetate

Identifiers

PMID19762470
PMCPMC2797261
OpenAlexW2089959534

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.