Evidence map›Paper›PMID 25675300›Full record

ArticleCell death & disease2015

Pin1 inhibits PP2A-mediated Rb dephosphorylation in regulation of cell cycle and S-phase DNA damage.

Y Tong, H Ying, R Liu, L Li, J Bergholz, Z-X Xiao

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
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  5. Review
  6. Expression and significance of pin1 in the wound healing.Archives of dermatological research · 2024
    Article
  7. Review
  8. Review
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  11. Review
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  13. Article
  14. Article
  15. Review
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  17. Review
  18. PIN1 in Cell Cycle Control and Cancer.Frontiers in pharmacology · 2018
    Review
  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

6 authors at 3 institutions in 2 countries.

Y TongCenter of Growth, Metabolism and Aging, Key Laboratory of Biological Resources and Ecological Environment of Ministry of Education, College of Life Sciences and State Key Laboratory of Biotherapy, Sichuan University, Chengdu 610064, China.
H YingThe University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
R LiuCenter of Growth, Metabolism and Aging, Key Laboratory of Biological Resources and Ecological Environment of Ministry of Education, College of Life Sciences and State Key Laboratory of Biotherapy, Sichuan University, Chengdu 610064, China.
L LiCancer Center, West China Hospital, Sichuan University, Chengdu 610041, China.
J BergholzCenter of Growth, Metabolism and Aging, Key Laboratory of Biological Resources and Ecological Environment of Ministry of Education, College of Life Sciences and State Key Laboratory of Biotherapy, Sichuan University, Chengdu 610064, China.
Z-X Xiao1] Center of Growth, Metabolism and Aging, Key Laboratory of Biological Resources and Ecological Environment of Ministry of Education, College of Life Sciences and State Key Laboratory of Biotherapy, Sichuan University, Chengdu 610064, China [2] Department of Biochemistry, Boston University School of Medicine, Boston, MA 02118, USA.
Sichuan University · CNBoston University · USThe University of Texas MD Anderson Cancer Center · US

Funding

Role of MDM2 in Cell Proliferation and TumorigenesisR01CA079804 · NCI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI XIAO, ZHI-XIONG JIM · 1999 to 2010
$2.2M
NCI NIH HHS CA79804NCI NIH HHS R01 CA079804
6 · The paper itself

Abstract

Inactivation of the retinoblastoma protein (Rb) has a key role in tumorigenesis. It is well established that Rb function is largely regulated by a dynamic balance of phosphorylation and dephosphorylation. Although much research has been done to understand the mechanisms and function of RB phosphorylation, the regulation of Rb dephosphorylation is still not well understood. In this study, we demonstrate that Pin1 has an important role in the regulation of Rb function in cell cycle progression and S-phase checkpoint upon DNA damage. We show that the Rb C-pocket directly binds to the Pin1 WW domain in vitro and in vivo, and that the phosphorylation of Rb C-pocket by G1/S Cyclin/Cyclin-dependent kinase complexes is critical for mediating this interaction. We further show that Rb-mediated cell cycle arrest and Rb-induced premature cellular senescence are effectively inhibited by Pin1 expression. In addition, DNA damage induces Rb dephosphorylation in a PP2A-dependent manner, and this process is inhibited by Pin1. Furthermore, the overexpression of Pin1 promotes Rb hyperphosphorylation upon S-phase DNA damage. Importantly, both the Pin1 WW domain and isomerase activity are required for its effect on S-phase checkpoint. Moreover, the overexpression of Pin1 is correlated with Rb hyperphosphorylation in breast cancer biopsies. These results indicate that Pin1 has a critical role in the modulation of Rb function by the regulation of Rb dephosphorylation, which may have an important pathological role in cancer development.

Indexed as

Cell CycleCell Line, TumorDNA DamageFlow CytometryHumansImmunohistochemistryImmunoprecipitationNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphorylationProtein Phosphatase 2Retinoblastoma ProteinNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePIN1 protein, humanProtein Phosphatase 2Retinoblastoma Protein

Identifiers

PMID25675300
PMCPMC4669794
OpenAlexW1977306573

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.