Evidence map›Paper›PMID 16936753›Full record

ReviewOncogene2006

Rb2/p130 and protein phosphatase 2A: key mediators of ovarian carcinoma cell growth suppression by all-trans retinoic acid.

K J Soprano, E Purev, S Vuocolo, D R Soprano

Abstract readReview
PubMed Publisher
In one paragraph

Review in Oncogene, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
1.6field-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

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.

  1. Genetic variations in cancer-related significantly mutated genes and lung cancer susceptibility.Annals of oncology : official journal of the European Society for Medical Oncology · 2017
    Pooled it
  2. Article
  3. Review
  4. Article
  5. Review
  6. Anti-tumour effects of all-trans retinoid acid on serous ovarian cancer.Journal of experimental & clinical cancer research : CR · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. PP2A as a master regulator of the cell cycle.Critical reviews in biochemistry and molecular biology
    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

4 authors at 1 institution in 1 country.

K J SopranoDepartment of Microbiology and Immunology, Temple University School of Medicine, Philadelphia, PA 19140, USA. sopranok@temple.edu
E Purev
S Vuocolo
D R Soprano
Temple University · US

Funding

RETINOIDS FOR TREATMENT OF OVARIAN CARCINOMAR01CA064945 · NCI · TEMPLE UNIV OF THE COMMONWEALTH · PI SOPRANO, KENNETH J · 1994 to 2007
$1.9M
NCI NIH HHS CA 64945
6 · The paper itself

Abstract

Despite a number of attempts to improve treatment of ovarian cancer, it remains the most common cause of death from gynecological cancers. Thus, it is very important to identify more effective drugs for treatment and prevention of ovarian cancer. All-trans-retinoic acid (ATRA) has been shown to arrest the growth of ovarian carcinoma cells in G0/G1 and to significantly elevate levels of Rb2/p130 protein, a member of the retinoblastoma family of tumor suppressors. As ATRA treatment leads to a significant increase in the amount of Rb2/p130 protein but not mRNA, the elevated levels of Rb2/p130 protein is likely the result of increased stability. In studies to elucidate the mechanism by which ATRA alters Rb2/p130 stability in ovarian cancer cells, it was determined that PP2A, a serine/threonine phosphatase, binds and dephosphorylates Rb2/p130. Dephosphorylated Rb2/p130 exhibits decreased ubiquitination and thus is not degraded by the proteasome. The sites at which PP2A catalytic subunit (PP2Ac) interacts with Rb2/p130 have been localized to the NLS in the C-terminus of Rb2/p130. These sites are also involved in the interaction of Rb/p130 with importin beta and importin alpha, members of the nuclear transport machinery. It is known that importin alpha recognizes a NLS on a target protein and importin beta binds the nuclear pore complex. Moreover, it has been shown that the binding of importin alpha to NLS significantly decreases with phosphorylation of NLS. In ATRA-treated ovarian carcinoma cells, PP2A binds to Rb2/p130 and dephosphorylates the NLS of Rb2/p130 leading to the interaction of importin alpha with Rb2/p130. Importin beta then binds to the importin alpha-Rb2/p130 complex, leading to the translocation of the Rb2/p130 to the nucleus where it acts to arrest ovarian cancer cells in G1 and suppress proliferation.

Indexed as

Antineoplastic AgentsCell DivisionCell NucleusFemaleHumansOvarian NeoplasmsPhosphoprotein PhosphatasesProtein Phosphatase 2Protein TransportRetinoblastoma-Like Protein p130RetinoidsTretinoinAntineoplastic AgentsPhosphoprotein PhosphatasesProtein Phosphatase 2Retinoblastoma-Like Protein p130RetinoidsTretinoin

Identifiers

PMID16936753
OpenAlexW1966603980

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.