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Yeast As a Chassis for Developing Functional Assays to Study Human P53
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Phosphomimetic Mutation Destabilizes the Central Core Domain of Human p53

Johnson Wahengbam Luwang1, Ramanathan Natesh1

  • 1School of Biology, Indian Institute of Science Education and Research Thiruvananthapuram, Thiruvananthapuram-695551, Kerala, India.

IUBMB Life
|August 31, 2018
PubMed

Insights

Aurora B kinase phosphorylation destabilizes the p53 protein, impacting its structure and DNA binding. This study reveals how these modifications affect p53

Area of Science:

  • Molecular Biology
  • Protein Biochemistry
  • Cancer Research

Background:

  • p53 protein activity is regulated by posttranslational modifications.
  • Aurora B kinase phosphorylation of p53 reduces its transcriptional activity and promotes degradation.

Purpose of the Study:

  • To investigate the structural and functional consequences of p53 phosphorylation by Aurora B kinase.
  • To characterize the biophysicochemical properties of p53 phosphomimetic mutants.

Main Methods:

  • Generation of five phosphomimetic mutants of the p53 core domain.
  • Biophysical characterization including thermal stability and DNA binding assays.

Main Results:

  • T211E, S215E, and S269E p53 mutants exhibited thermal instability and increased aggregation.
  • These mutants, along with S183E, showed impaired DNA binding compared to wild-type (WT) p53.
  • Phosphomimetic substitution led to structural and functional destabilization of p53.

Conclusions:

  • Phosphorylation by Aurora B kinase induces significant structural and functional changes in p53.
  • These findings provide molecular insights into p53 regulation and degradation pathways.
Keywords:
EMSAaggregationfluorescencephosphomimetic

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