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Phosphorylation of BRCA2 by the Polo-like kinase Plk1 is regulated by DNA damage and mitotic progression

MiYoung Lee1, Matthew J Daniels, Ashok R Venkitaraman

  • 1CR UK Department of Oncology and the Medical Research Council Cancer Cell Unit, Hutchison/MRC Research Centre, University of Cambridge, Hills Road, Cambridge CB2 2XZ, UK.

Oncogene
|December 3, 2003
PubMed

Insights

Researchers found that the breast cancer protein BRCA2 is phosphorylated by the mitotic kinase Plk1 during cell division. This Plk1-mediated BRCA2 modification is responsive to DNA damage and mitotic progression.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • BRCA2 is crucial for chromosomal stability and DNA repair.
  • Post-translational modifications of BRCA2 are not well understood.
  • Polo-like kinase 1 (Plk1) is a key regulator of mitosis.

Purpose of the Study:

  • To investigate the role of Plk1 in BRCA2 regulation.
  • To characterize the post-translational modification of BRCA2 by Plk1.

Main Methods:

  • Cell synchronization and treatment with RNA interference to deplete Plk1.
  • Co-immunoprecipitation to assess BRCA2-Plk1 interaction.
  • Analysis of BRCA2 phosphorylation sites within the BRC repeat region.

Main Results:

  • BRCA2 is phosphorylated by Plk1 during the G2/M cell cycle phases.
  • Plk1 depletion inhibits BRCA2 phosphorylation.
  • BRCA2 and Plk1 interact via a conserved region in BRCA2.
  • Plk1 phosphorylates residues between BRC repeats.
  • Adriamycin treatment inhibits Plk1-mediated BRCA2 phosphorylation.

Conclusions:

  • A regulatory circuit involving Plk1-mediated phosphorylation of BRCA2 is identified.
  • This circuit is sensitive to both mitotic progression and DNA damage.
  • Findings provide new insights into BRCA2 regulation and its role in maintaining genomic integrity.

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