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Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery

Libor Macůrek1, Arne Lindqvist, Dan Lim

  • 1Department of Medical Oncology, University Medical Center Utrecht, Utrecht 3584CG, The Netherlands.

Nature
|July 11, 2008
PubMed

Insights

Aurora A kinase directly phosphorylates Polo-like kinase-1 (PLK1) at Thr 210, enabling cell division. This activation, enhanced by Bora, is crucial for mitotic entry following checkpoint arrest.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Polo-like kinase-1 (PLK1) is vital for cell division.
  • PLK1 activation requires phosphorylation at Thr 210, but the responsible kinase is unknown.

Purpose of the Study:

  • Identify the kinase responsible for PLK1 activation.
  • Elucidate the role of Aurora A and Bora in PLK1 phosphorylation and mitotic entry.

Main Methods:

  • Phosphorylation assays in human cells.
  • Analysis of PLK1 activation during the cell cycle.
  • Use of phospho-mimicking PLK1 mutants.

Main Results:

  • Aurora A (AURKA) directly phosphorylates PLK1 at Thr 210.
  • Bora enhances AURKA activity towards PLK1.
  • AURKA-dependent PLK1 phosphorylation is essential for mitotic entry after checkpoint arrest.
  • A PLK1 phospho-mimicking mutant partially rescues checkpoint recovery.

Conclusions:

  • Aurora A is the primary kinase responsible for initiating PLK1 activation.
  • The Bora/Aurora A complex plays a critical role in regulating PLK1 activity for cell cycle progression.

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