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Cancer Osaka thyroid (Cot) phosphorylates Polo-like kinase (PLK1) at Ser137 but not at Thr210

Binhui Wu1, Ping Jiang, Yuguang Mu

  • 1School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.

Biological Chemistry
|October 7, 2009
PubMed

Insights

Cancer Osaka thyroid (Cot) kinase phosphorylates Polo-like kinase 1 (Plk1) at Ser137. This discovery reveals a new upstream regulatory mechanism for Plk1

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Oncology

Background:

  • Cancer Osaka thyroid (Cot) is a proto-oncogenic kinase within the MAP3K family.
  • Understanding kinase interactions is crucial for deciphering cellular regulation and oncogenic pathways.

Purpose of the Study:

  • To investigate the potential of Cot kinase as an upstream regulator of Polo-like kinase 1 (Plk1).
  • To identify specific phosphorylation sites targeted by Cot on Plk1.

Main Methods:

  • Peptide-based substrate screening assays.
  • Kinase assays using intact Plk1 and synthetic peptides.
  • 3D peptide structure prediction and Cot-Plk1 interaction modeling.
  • In vivo experiments including Cot knockdown in HeLa cells.

Main Results:

  • Cot kinase was identified to phosphorylate Plk1 specifically at Serine 137 (Ser137).
  • Phosphorylation at Threonine 210 (Thr210) was not observed.
  • In vivo experiments confirmed Cot's ability to phosphorylate Ser137, and its knockdown reduced Ser137 phosphorylation levels.

Conclusions:

  • Cot kinase acts as an upstream kinase for Plk1, phosphorylating it at Ser137.
  • This finding suggests a novel regulatory mechanism controlling Plk1's cellular functions.
  • Further research into the Cot-Plk1 pathway may reveal new therapeutic targets in cancer.

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