Evidence map›Paper›PMID 19121998›Full record

ArticleThe Journal of biological chemistry2009

Phosphorylation of p53 is regulated by TPX2-Aurora A in xenopus oocytes.

Gaetan Pascreau, Frank Eckerdt, Andrea L Lewellyn, Claude Prigent, James L Maller

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

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  17. Overexpression of Aurora-A promotes laryngeal cancer progression by enhancing invasive ability and chromosomal instability.European archives of oto-rhino-laryngology : official journal of the European Federation of Oto-Rhino-Laryngological Societies (EUFOS) : affiliated with the German Society for Oto-Rhino-Laryngology - Head and Neck Surgery · 2012
    Article
  18. Aurora kinase A promotes ovarian tumorigenesis through dysregulation of the cell cycle and suppression of BRCA2.Clinical cancer research : an official journal of the American Association for Cancer Research · 2010
    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 2 institutions in 2 countries.

Gaetan PascreauHoward Hughes Medical Institute and Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado 80045, USA.
Frank Eckerdt
Andrea L Lewellyn
Claude Prigent
James L Maller
Howard Hughes Medical Institute · USCentre National de la Recherche Scientifique · FR

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

p53 is an important tumor suppressor regulating the cell cycle at multiple stages in higher vertebrates. The p53 gene is frequently deleted or mutated in human cancers, resulting in loss of p53 activity. This leads to centrosome amplification, aneuploidy, and tumorigenesis, three phenotypes also observed after overexpression of the oncogenic kinase Aurora A. Accordingly, recent studies have focused on the relationship between these two proteins. p53 and Aurora A have been reported to interact in mammalian cells, but the function of this interaction remains unclear. We recently reported that Xenopus p53 can inhibit Aurora A activity in vitro but only in the absence of TPX2. Here we investigate the interplay between Xenopus Aurora A, TPX2, and p53 and show that newly synthesized TPX2 is required for nearly all Aurora A activation and for full p53 synthesis and phosphorylation in vivo during oocyte maturation. In vitro, phosphorylation mediated by Aurora A targets serines 129 and 190 within the DNA binding domain of p53. Glutathione S-transferase pull-down studies indicate that the interaction occurs via the p53 transactivation domain and the Aurora A catalytic domain around the T-loop. Our studies suggest that targeting of TPX2 might be an effective strategy for specifically inhibiting the phosphorylation of Aurora A substrates, including p53.

Indexed as

AnimalsAurora KinasesCell Cycle ProteinsFemaleGlutathione TransferaseImmunoprecipitationMicrotubule-Associated ProteinsNuclear ProteinsOocytesPhosphoproteinsPhosphorylationProtein Serine-Threonine KinasesRecombinant ProteinsTranscriptional ActivationTumor Suppressor Protein p53Xenopus laevisAurora KinasesCell Cycle ProteinsGlutathione TransferaseMicrotubule-Associated ProteinsNuclear ProteinsPhosphoproteinsProtein Serine-Threonine KinasesRecombinant ProteinsTPX2 protein, XenopusTumor Suppressor Protein p53Xenopus Proteins

Identifiers

PMID19121998
PMCPMC2645813
OpenAlexW2028925508

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.