Evidence map›Paper›PMID 24501426›Full record

ArticleMolecular biology of the cell2014

Nek2 phosphorylates and stabilizes β-catenin at mitotic centrosomes downstream of Plk1.

Bertrade C Mbom, Kathleen A Siemers, Maggie A Ostrowski, W James Nelson, Angela I M Barth

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
2.8field-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

66 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
  2. NEK2 drives pathogenesis, drug resistance, and LMP1 expression in EBV-positive non-Hodgkin lymphoma.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. The NIMA-related kinase family and cancer.Frontiers in oncology · 2025
    Review
  10. Article
  11. Role of NEK2 in tumorigenesis and tumor progression.Trends in molecular medicine · 2025
    Review
  12. Article
  13. Article
  14. Review
  15. The interplay between Wnt signaling pathways and microtubule dynamics.In vitro cellular & developmental biology. Animal · 2024
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

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

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.

Bertrade C MbomDepartment of Biology, Stanford University, Stanford, CA 94305 Department of Chemical Engineering, Stanford University, Stanford, CA 94305 Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305.
Kathleen A Siemers
Maggie A Ostrowski
W James Nelson
Angela I M Barth
Stanford University · US

Funding

Topogenesis of NA/K-ATPASE in Polarized Epithelial CellsR37GM035527 · NIGMS · STANFORD UNIVERSITY · PI NELSON, W. JAMES · 2003 to 2012
$7.4M
Topogenesis of Na/K-ATPase in Polarized MDCK Epithelial CellsR01GM035527 · NIGMS · STANFORD UNIVERSITY · PI NELSON, W. JAMES · 1986 to 2015
$3.3M
NIGMS NIH HHS GM35527NIGMS NIH HHS R01 GM035527NIGMS NIH HHS R37 GM035527
6 · The paper itself

Abstract

β-Catenin is a multifunctional protein with critical roles in cell-cell adhesion, Wnt signaling, and the centrosome cycle. Whereas the regulation of β-catenin in cell-cell adhesion and Wnt signaling are well understood, how β-catenin is regulated at the centrosome is not. NIMA-related protein kinase 2 (Nek2), which regulates centrosome disjunction/splitting, binds to and phosphorylates β-catenin. Using in vitro and cell-based assays, we show that Nek2 phosphorylates the same regulatory sites in the N-terminus of β-catenin as glycogen synthase kinase 3β (GSK3β), which are recognized by a specific phospho-S33/S37/T41 antibody, as well as additional sites. Nek2 binding to β-catenin appears to inhibit binding of the E3 ligase β-TrCP and prevents β-catenin ubiquitination and degradation. Thus β-catenin phosphorylated by Nek2 is stabilized and accumulates at centrosomes in mitosis. We further show that polo-like kinase 1 (Plk1) regulates Nek2 phosphorylation and stabilization of β-catenin. Taken together, these results identify a novel mechanism for regulating β-catenin stability that is independent of GSK3β and provide new insight into a pathway involving Plk1, Nek2, and β-catenin that regulates the centrosome cycle.

Indexed as

Mitosisbeta CateninCasein Kinase ICell Cycle ProteinsCentrosomeGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHCT116 CellsHEK293 CellsHumansNIMA-Related KinasesPhosphorylationPolo-Like Kinase 1Protein Serine-Threonine KinasesProtein StabilityProto-Oncogene Proteinsbeta CateninCasein Kinase ICell Cycle ProteinsGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaGSK3B protein, humanNEK2 protein, humanNIMA-Related KinasesPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsSerine

Identifiers

PMID24501426
PMCPMC3967981
OpenAlexW2147399984

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.