Evidence map›Paper›PMID 16501611›Full record

ArticleOncogene2006

Protein serine/threonine phosphatase-1 dephosphorylates p53 at Ser-15 and Ser-37 to modulate its transcriptional and apoptotic activities.

D W-C Li, J-P Liu, P C Schmid, R Schlosser, H Feng, W-B Liu, Q Yan, L Gong, S-M Sun, M Deng and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.1field-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

49 citing papers in PubMed, 92 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Deciphering the PTM codes of the tumor suppressor p53.Journal of molecular cell biology · 2022
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. The Clinical Significance ofOncoTargets and therapy · 2020
    Article
  19. Article
  20. 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

11 authors at 4 institutions in 2 countries.

D W-C LiThe Hormel Institute, University of Minnesota, Austin, 55912, USA. dwli1688@hotmail.com
J-P Liu
P C Schmid
R Schlosser
H Feng
W-B Liu
Q Yan
L Gong
S-M Sun
M Deng
Y Liu
Hunan Normal University · CNHormel (United States) · USUniversity of Minnesota · USTwin Cities Orthopedics · US

Funding

Antiapoptotic Mechanism of Protein Phosphatase-1 in LensR01EY015765 · NEI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI LI, DAVID W · 2005 to 2007
$873k
NEI NIH HHS EY15765NEI NIH HHS R01 EY015765
6 · The paper itself

Abstract

We have previously demonstrated that the serine/threonine protein phosphatase-1 (PP-1) plays an important role in promoting cell survival. However, the molecular mechanisms by which PP-1 promotes survival remain largely unknown. In the present study, we provide evidence to show that PP-1 can directly dephosphorylate a master regulator of apoptosis, p53, to negatively modulate its transcriptional and apoptotic activities, and thus to promote cell survival. As a transcriptional factor, the function of p53 can be greatly regulated by phosphorylation and dephosphorylation. While the kinases responsible for phosphorylation of the 17 serine/threonine sites have been identified, the dephosphorylation of these sites remains largely unknown. In the present study, we demonstrate that PP-1 can dephosphorylate p53 at Ser-15 and Ser-37 through co-immunoprecipitation, in vitro and in vivo dephosphorylation assays, overexpression and silence of the gene encoding the catalytic subunit for PP-1. We further show that mutations mimicking constitutive dephosphorylation or phosphorylation of p53 at these sites attenuate or enhance its transcriptional activity, respectively. As a result of the changed p53 activity, expression of the downstream apoptosis-related genes such as bcl-2 and bax is accordingly altered and the apoptotic events are either largely abrogated or enhanced. Thus, our results demonstrate that PP-1 directly dephosphorylates p53, and dephosphorylation of p53 has as important impact on its functions as phosphorylation does. In addition, our results reveal that one of the molecular mechanisms by which PP-1 promotes cell survival is to dephosphorylate p53, and thus negatively regulate p53-dependent death pathway.

Indexed as

Amino Acid SubstitutionAnimalsApoptosisbcl-2-Associated X ProteinCell LineEpithelial CellsGenes, bcl-2Genes, p53Genes, ReporterHumansImmunoprecipitationLens, CrystallineMarine ToxinsMiceMice, KnockoutOkadaic Acidbcl-2-Associated X Proteincalyculin AMarine ToxinsOkadaic AcidOxazolesPhosphoprotein PhosphatasesPhosphoserineProtein Phosphatase 1Proto-Oncogene Proteins c-bcl-2Recombinant Fusion ProteinsRNA, Small InterferingTumor Suppressor Protein p53

Identifiers

PMID16501611
OpenAlexW2040331457

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.