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Decrease of mitochondrial p53 during late apoptosis is linked to its dephosphorylation on serine 20.

Cédric Castrogiovanni1,2, Marie Vandaudenard1, Béranger Waterschoot3

  • 1a Laboratory of Molecular and Cellular Biology; Institute of Life Sciences; Université Catholique de Louvain ; Louvain-la-Neuve , Belgium.

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Summary
This summary is machine-generated.

Genotoxic stress triggers tumor suppressor p53 mitochondrial translocation for apoptosis. Serine 20 phosphorylation influences p53

Keywords:
BAKapoptosiscaspasemitochondriap53phosphorylationserine 20

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The tumor suppressor p53 plays a critical role in apoptosis induction.
  • p53 translocates to mitochondria to interact with BCL-2 family proteins (BAK, BAX) during genotoxic stress.

Purpose of the Study:

  • To investigate the kinetics of p53 mitochondrial translocation.
  • To determine the role of serine 20 phosphorylation in p53's mitochondrial localization and function during apoptosis.

Main Methods:

  • Analysis of p53 mitochondrial translocation kinetics in HCT-116 and PA-1 cells.
  • Exposure to genotoxic stresses (doxorubicin, camptothecin, UVB).
  • Assessment of p53 phosphorylation at serine 20 and its correlation with mitochondrial levels.

Main Results:

  • Mitochondrial p53 levels increase early after stress, peak, then decrease.
  • Serine 20 phosphorylated p53 is found in mitochondria.
  • Decreased Ser-20 phosphorylation correlates with reduced mitochondrial p53 during late apoptosis.
  • S20A p53 mutant shows impaired late-stage mitochondrial localization and BAK interaction.
  • A 45 kDa caspase-cleaved p53 fragment is identified in cytosolic and mitochondrial fractions.

Conclusions:

  • Serine 20 phosphorylation is crucial for maintaining p53's mitochondrial localization in late apoptosis.
  • Caspase-mediated cleavage of p53 generates a novel fragment during apoptosis.