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Plk2 regulates centriole duplication through phosphorylation-mediated degradation of Fbxw7 (human Cdc4)

Onur Cizmecioglu1, Annekatrin Krause, Ramona Bahtz

  • 1Cell cycle Control and Carcinogenesis (F045), German Cancer Research Center (DKFZ), Im Neuenheimer Feld 242, 69120 Heidelberg, Germany.

Journal of Cell Science
|March 9, 2012
PubMed

Insights

Polo-like kinase 2 (Plk2) targets F-box/WD repeat-containing protein 7 (Fbxw7), stabilizing cyclin E. This Plk2-Fbxw7 interaction is crucial for regulating centrosome duplication at the start of the S phase.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Polo-like kinases (Plks) are essential regulators of cell division processes, including mitosis, cytokinesis, and centriole duplication.
  • Plk2 specifically is activated during the G1 phase and plays a key role in centrosome reproduction, but the underlying mechanisms remain unclear.

Purpose of the Study:

  • To elucidate the molecular mechanisms by which Plk2 regulates centriole duplication.
  • To identify direct targets of Plk2 involved in centrosome reproduction.

Main Methods:

  • In vitro and in vivo protein interaction studies.
  • Phosphorylation site analysis (serine 176).
  • Ubiquitin-mediated degradation assays.
  • Cellular studies involving Fbxw7 depletion in human cells.

Main Results:

  • Plk2 directly targets and phosphorylates the F-box protein Fbxw7 at serine 176.
  • Plk2 and Fbxw7 form a complex, leading to Fbxw7 destabilization and subsequent accumulation of cyclin E.
  • Loss of Fbxw7 function results in uncontrolled centriole duplication in human cells.

Conclusions:

  • A novel Plk2-dependent pathway regulating centrosome duplication and the onset of S phase has been identified.
  • Plk2-mediated phosphorylation of Fbxw7 is critical for controlling cyclin E levels and preventing aberrant centriole replication.

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