Evidence map›Paper›PMID 27240320›Full record

ArticleNature cell biology2016

Pten regulates spindle pole movement through Dlg1-mediated recruitment of Eg5 to centrosomes.

Janine H van Ree, Hyun-Ja Nam, Karthik B Jeganathan, Arun Kanakkanthara, Jan M van Deursen

Open access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed, 1 pooled it
5.5field-weighted citation impact, top 4% 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

42 citing papers in PubMed, 1 synthesis or guideline pooled it, 62 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Kinesin Spindle Protein (KIF11) in Mitosis and Cancer.International journal of molecular sciences · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. The two sides of chromosomal instability: drivers and brakes in cancer.Signal transduction and targeted therapy · 2024
    Review
  10. Review
  11. Article
  12. PTEN-Long inhibits the biological behaviors of glioma cells.American journal of translational research · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  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

5 authors at 1 institution in 1 country.

Janine H van ReeDepartments of Pediatric and Adolescent Medicine, Mayo Clinic College of Medicine, Rochester, Minnesota 55905, USA.
Hyun-Ja NamDepartments of Pediatric and Adolescent Medicine, Mayo Clinic College of Medicine, Rochester, Minnesota 55905, USA.
Karthik B JeganathanDepartments of Pediatric and Adolescent Medicine, Mayo Clinic College of Medicine, Rochester, Minnesota 55905, USA.
Arun KanakkantharaDepartments of Pediatric and Adolescent Medicine, Mayo Clinic College of Medicine, Rochester, Minnesota 55905, USA.
Jan M van DeursenDepartments of Pediatric and Adolescent Medicine, Mayo Clinic College of Medicine, Rochester, Minnesota 55905, USA.
Mayo Clinic · US

Funding

Role of PTEN in Chromosome Segregation and its Importance for Tumor SuppressionR01CA168709 · NCI · MAYO CLINIC ROCHESTER · PI VAN DEURSEN, JAN M. · 2012 to 2016
$1.6M
NCI NIH HHS R01 CA168709
6 · The paper itself

Abstract

Phosphatase and tensin homologue (Pten) suppresses neoplastic growth by negatively regulating PI(3)K signalling through its phosphatase activity. To gain insight into the actions of non-catalytic Pten domains in normal physiological processes and tumorigenesis, we engineered mice lacking the PDZ-binding domain (PDZ-BD). Here, we show that the PDZ-BD regulates centrosome movement and that its heterozygous or homozygous deletion promotes aneuploidy and tumour formation. We found that Pten is recruited to pre-mitotic centrosomes in a Plk1-dependent fashion to create a docking site for protein complexes containing the PDZ-domain-containing protein Dlg1 (also known as Sap97) and Eg5 (also known as Kif11), a kinesin essential for centrosome movement and bipolar spindle formation. Docking of Dlg1-Eg5 complexes to Pten depended on Eg5 phosphorylation by the Nek9-Nek6 mitotic kinase cascade and Cdk1. PDZ-BD deletion or Dlg1 ablation impaired loading of Eg5 onto centrosomes and spindle pole motility, yielding asymmetrical spindles that are prone to chromosome missegregation. Collectively, these data demonstrate that Pten, through the Dlg1-binding ability of its PDZ-BD, accumulates phosphorylated Eg5 at duplicated centrosomes to establish symmetrical bipolar spindles that properly segregate chromosomes, and suggest that this function contributes to tumour suppression.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCell CycleCentrosomeDiscs Large Homolog 1 ProteinHumansKinesinsMembrane ProteinsMiceMitosisNerve Tissue ProteinsPTEN PhosphohydrolaseSAP90-PSD95 Associated ProteinsSpindle PolesAdaptor Proteins, Signal TransducingDiscs Large Homolog 1 ProteinDLG1 protein, humanDlg1 protein, mouseKIF11 protein, humanKif11 protein, mouseKinesinsMembrane ProteinsNerve Tissue ProteinsPTEN PhosphohydrolasePTEN protein, humanPten protein, mouseSAP90-PSD95 Associated Proteins

Identifiers

PMID27240320
PMCPMC5004208
OpenAlexW2403508573

What OpenQuestion holds

Textmetadata
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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.