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Purification of Ubiquitinated p53 Proteins from Mammalian Cells
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Purification of Ubiquitinated p53 Proteins from Mammalian Cells

Published on: March 21, 2022

Aurora A mediates cross-talk between N- and C-terminal post-translational modifications of p53

Lorna Jane Warnock1, Sally Anne Raines, Jo Milner

  • 1YCR p53 Research Unit, Department of Biology, University of York, York, UK.

Cancer Biology & Therapy
|December 14, 2011
PubMed

Insights

Aurora A kinase regulates tumor suppressor p53 levels and expression. This interaction impacts p53

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Cancer Biology

Background:

  • Aurora A kinase phosphorylates tumor suppressor p53 at Serine 215, inhibiting its transcriptional activity.
  • The interaction between Aurora A and p53 is crucial in cellular regulation and cancer development.

Purpose of the Study:

  • To investigate the reciprocal regulatory relationship between Aurora A and p53.
  • To explore the impact of Aurora A on p53 protein levels and post-translational modifications.
  • To assess the relevance of p53's conformational state in targeted cancer therapies.

Main Methods:

  • Utilized isogenic p53 wild-type and p53-null colorectal carcinoma cells.
  • Employed immunoblotting to detect p53 and Aurora A protein levels.
  • Analyzed p53 phosphorylation at Serine 215 (S215) and Serine 37 (S37) and PAb240 antibody reactivity.

Main Results:

  • Demonstrated that Aurora A positively regulates human p53 protein levels.
  • Showed that p53 reciprocally regulates human Aurora A protein expression.
  • Found no correlation between S215 phosphorylation and PAb240 recognition, but S37 phosphorylation correlated with PAb240 reactivity.
  • Provided evidence for Aurora A-mediated cross-talk between N- and C-terminal p53 post-translational modifications.

Conclusions:

  • The reciprocal relationship between Aurora A and p53 influences their respective protein levels and modifications.
  • Aurora A-induced post-translational modifications of p53, particularly at S37, may affect p53's conformation and antibody recognition.
  • Understanding this interplay is critical for developing effective p53- and Aurora A-targeted anticancer therapies.

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