Evidence map›Paper›PMID 22562304›Full record

ArticleMolecular and cellular biochemistry2012

TPA-induced cell transformation provokes a complex formation between Pin1 and 90 kDa ribosomal protein S6 kinase 2.

Young Sik Cho, Seung Yeon Park, Dong Joon Kim, Sang-Han Lee, Kee-Min Woo, Kyung-Ae Lee, Yoon-Jin Lee, Yong-Yeon Cho, Jung-Hyun Shim

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In one paragraph

Article in Molecular and cellular biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

20 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Pin1 and Alzheimer's disease.Translational research : the journal of laboratory and clinical medicine · 2023
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Post-translational Modifications of the Peptidyl-Prolyl Isomerase Pin1.Frontiers in cell and developmental biology · 2020
    Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Review
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  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

9 authors at 4 institutions in 2 countries.

Young Sik ChoDepartment of Pharmacy, Keimyung University, Dalseo-gu, Taegu, Republic of Korea.
Seung Yeon Park
Dong Joon Kim
Sang-Han Lee
Kee-Min Woo
Kyung-Ae Lee
Yoon-Jin Lee
Yong-Yeon Cho
Jung-Hyun Shim
Soonchunhyang University · KRCatholic University of Korea · KRHormel (United States) · USKeimyung University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modification of peptidyl cis/trans prolyl isomerase Pin1 is crucial in regulation of gene stability. Pin1 phosphorylation at Ser(16) has been regarded as a marker for Pin1 isomerase activity and introduction of phosphorylation on Ser/Thr-Pro of substrate proteins is prerequisite for its binding activity with Pin1 and subsequent isomerization. Here, we found that 90 kDa ribosomal protein S6 kinase 2 (RSK2) could form a physical complex with Pin1, leading to phosphorylation of Pin1 at Ser(16) ex vivo and in vitro respectively. Intriguingly, Pin1(+/+) mouse embryonic fibroblasts (MEFs) exhibited significantly an increase in 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced RSK2 phosphorylation with a marginal Pin1 phosphorylation compared with Pin1(-/-) MEFs. Moreover, TPA-induced Ser(16) Pin1 phosphorylation as well as RSK2 phosphorylation was considerably profound in RSK(+/+) MEFs but not in RSK(-/-) MEFs. Consequently, knockdown of Pin1 using shRNA-Pin1 suppressed TPA-induced cell transformation in JB6 CI41 cells. Overall, these results indicate that Pin1 plays a critical role in TPA-induced tumorigenesis plausibly via physical interaction with RSK2 and reciprocal phosphorylation, therefore suggesting a potential therapeutic target for cancer treatment.

Indexed as

AnimalsCells, CulturedCell Transformation, NeoplasticEnzyme ActivationHumansMiceNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphorylationProtein BindingProtein Interaction MappingProtein Processing, Post-TranslationalRibosomal Protein S6 Kinases, 90-kDaTetradecanoylphorbol AcetateNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePIN1 protein, humanPin1 protein, mouseribosomal protein S6 kinase, 90kDa, polypeptide 3Ribosomal Protein S6 Kinases, 90-kDaTetradecanoylphorbol Acetate

Identifiers

PMID22562304
OpenAlexW2072936149

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.