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Phosphorylation by Aurora B kinase regulates caspase-2 activity and function.

Yoon Lim1, Dylan De Bellis2, Jarrod J Sandow3,4

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Mitotic catastrophe elimination of defective cells is regulated by caspase-2. Aurora B kinase (AURKB) phosphorylates caspase-2 at S384, blocking its apoptotic function during mitosis.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Mitotic catastrophe (MC) eliminates cells with abnormal chromosome numbers during mitosis.
  • Caspase-2 activation is crucial for MC, triggering apoptosis or cell cycle arrest.
  • The precise regulation of caspase-2 activation and function in MC remains incompletely understood.

Purpose of the Study:

  • To elucidate the molecular mechanisms governing caspase-2 activation and function during mitosis.
  • To identify regulatory post-translational modifications of caspase-2.
  • To investigate the role of mitotic kinases in controlling caspase-2 activity.

Main Methods:

  • Phosphoproteomic analysis to identify caspase-2 phosphorylation sites.
  • Site-directed mutagenesis to assess the functional impact of phosphorylation.
  • Biochemical assays to measure caspase-2 catalytic activity and apoptosis induction.
  • Molecular modeling to predict effects on substrate binding.

Main Results:

  • Six novel phosphorylation sites on caspase-2 were identified.
  • Aurora B kinase (AURKB) was found to phosphorylate caspase-2 at serine 384 (S384).
  • Phosphorylation at S384 inhibits caspase-2's catalytic activity and apoptosis-inducing function during mitotic stress, without affecting dimerization.
  • Molecular modeling suggests S384 phosphorylation may impede substrate binding.

Conclusions:

  • Caspase-2 S384 phosphorylation by AURKB is a key regulatory mechanism controlling caspase-2 activation.
  • This phosphorylation event acts as an inhibitory switch, preventing inappropriate caspase-2 activity during mitosis.
  • Understanding this regulation provides insights into the oncosuppressive role of mitotic catastrophe.