Evidence map›Paper›PMID 23633483›Full record

ArticleCancer research2013

SENP1 deSUMOylates and regulates Pin1 protein activity and cellular function.

Chun-Hau Chen, Che-Chang Chang, Tae Ho Lee, Manli Luo, Pengyu Huang, Pei-Hsin Liao, Shuo Wei, Fu-An Li, Ruey-Hwa Chen, Xiao Zhen Zhou and 2 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Cancer research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

63 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
  2. Article
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  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. The molecular mechanisms of peptidyl-prolylFrontiers in pharmacology · 2024
    Review
  13. Pin1 and Alzheimer's disease.Translational research : the journal of laboratory and clinical medicine · 2023
    Review
  14. Article
  15. Cancer-Associated Dysregulation of Sumo Regulators: Proteases and Ligases.International journal of molecular sciences · 2022
    Review
  16. Review
  17. Review
  18. Article
  19. Review
  20. Article

3 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 2 countries.

Chun-Hau ChenDepartment of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215, USA.
Che-Chang Chang
Tae Ho Lee
Manli Luo
Pengyu Huang
Pei-Hsin Liao
Shuo Wei
Fu-An Li
Ruey-Hwa Chen
Xiao Zhen Zhou
Hsiu-Ming Shih
Kun Ping Lu
Institute of Biological Chemistry, Academia Sinica · TWTaipei Medical University · TWBeth Israel Deaconess Medical Center · US

Funding

Translational Researchin Aging Trainnig ProgramT32AG023480 · NIA · HEBREW REHABILITATION CENTER FOR AGED · PI LIPSITZ, LEWIS · 2004 to 2024
$7.6M
Role of the Prolyl Isomerase Pin1 in the Development and Treatment of AsthmaR01HL111430 · NHLBI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI LU, KUN PING · 2012 to 2015
$2.7M
Function and Regulation of the Phosphorylation-Specific Prolyl Isomerase Pin1R01CA167677 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI LU, KUN PING · 2012 to 2016
$1.9M
Pin1-dependent telomere regulation in aging and Alzheimer's diseaseR00AG033104 · NIA · BETH ISRAEL DEACONESS MEDICAL CENTER · PI LEE, TAE HO · 2011 to 2013
$733k
NCI NIH HHS R01 CA167677NCI NIH HHS R01CA167677NHLBI NIH HHS R01 HL111430NIA NIH HHS R00 AG033104NIA NIH HHS R00AG033104NIA NIH HHS T32 AG023480
6 · The paper itself

Abstract

The Pin1 prolyl isomerase regulates phosphorylation signaling by controlling protein conformation after phosphorylation, and its upregulation promotes oncogenesis via acting on numerous oncogenic molecules. SUMOylation and deSUMOylation are dynamic mechanisms regulating a spectrum of protein activities. The SUMO proteases (SENP) remove SUMO conjugate from proteins, and their expression is deregulated in cancers. However, nothing is known about the role of SUMOylation in regulating Pin1 function. Here, we show that Pin1 is SUMOylated on Lys6 in the WW domain and on Lys63 in the PPIase domain. Pin1 SUMOylation inhibits its protein activity and oncogenic function. We further identify that SENP1 binds to and deSUMOylates Pin1. Importantly, either overexpression of SENP1 or disruption of Pin1 SUMOylation promotes the ability of Pin1 to induce centrosome amplification and cell transformation. Moreover, SENP1 also increases Pin1 protein stability in cell cultures, and Pin1 levels are positively correlated with SENP1 levels in human breast cancer specimens. These results not only uncover Pin1 SUMOylation on Lys6/63 as a novel mechanism to inhibit its activity and function but also identify a critical role for SENP1-mediated deSUMOylation in promoting Pin1 function during tumorigenesis.

Indexed as

SumoylationAmino Acid SequenceAmino Acid SubstitutionAnimalsBreast NeoplasmsCell LineCell Transformation, NeoplasticCentrosomeChromosomal InstabilityCyclin D1Cysteine EndopeptidasesEndopeptidasesFemaleGene Knockdown TechniquesHumansMiceCyclin D1Cysteine EndopeptidasesEndopeptidasesNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePIN1 protein, humanPin1 protein, mouseSENP1 protein, human

Identifiers

PMID23633483
PMCPMC3818121
OpenAlexW2102379338

What OpenQuestion holds

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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.