Evidence map›Paper›PMID 17229885›Full record

ArticleMolecular biology of the cell2007

Functional interaction of Aurora-A and PP2A during mitosis.

Virginie Horn, Jacques Thélu, Alphonse Garcia, Corinne Albigès-Rizo, Marc R Block, Jean Viallet

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
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  5. Review
  6. Article
  7. Combining peptide TNIIIA2 with all-American journal of cancer research · 2019
    Article
  8. Article
  9. Review
  10. The Aurora kinase inhibitors in cancer research and therapy.Journal of cancer research and clinical oncology · 2016
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Aurora A kinase (AURKA) in normal and pathological cell division.Cellular and molecular life sciences : CMLS · 2013
    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

6 authors.

Virginie HornInstitut Albert Bonniot, Centre de Recherche Institut National de la Santé et de la Recherche Médicale, Université Joseph Fourier U 823, Equipe DySAD, Université Joseph Fourier Site Santé, BP 170, F38042, Grenoble Cedex 09, France.
Jacques Thélu
Alphonse Garcia
Corinne Albigès-Rizo
Marc R Block
Jean Viallet

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Entry into mitosis is a highly regulated process, promoted by the activated Cyclin B1/Cdk1 complex. Activation of this complex is controlled, in part, by the protein kinase Aurora-A, which is a member of a multigenic serine/threonine kinase family. In normal cells, Aurora-A activity is regulated, at least in part, by degradation through the APC-ubiquitin-proteasome pathway. It has recently been proposed that, in Xenopus, Aurora-A degradation can be inhibited by phosphorylation. It would thus be expected that a phosphatase activity would release this blockade at the end of mitosis. Here, we have shown that the protein phosphatase PP2A and Aurora-A are colocalized at the cell poles during mitosis in human cells and interact within the same complex. Using the PP2A inhibitor okadaic acid and an RNAi approach, we have shown that this interaction is functional within the cell. PP2A/Aurora-A interaction is promoted by an S51D mutation in Aurora-A and inhibited by a phosphomimetic peptide centered around Aurora-A S51, thereby strongly suggesting that PP2A controls Aurora-A degradation by dephosphorylating serine 51 in the A box of the human enzyme.

Indexed as

AnimalsAurora KinasesCatalytic DomainCentrosomeCHO CellsCricetinaeCricetulusEnzyme InhibitorsHumansMitosisOkadaic AcidPhosphoprotein PhosphatasesPhosphorylationProtein Serine-Threonine KinasesProtein SubunitsSerineAurora KinasesEnzyme InhibitorsOkadaic AcidPhosphoprotein PhosphatasesProtein Serine-Threonine KinasesProtein SubunitsSerine

Identifiers

PMID17229885
PMCPMC1839003

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.