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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Published on: May 3, 2018

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Oncogenic potential of BEX4 is conferred by Polo-like kinase 1-mediated phosphorylation

Jin-Kwan Lee1, Geun-Hyoung Ha2, Hyun-Soo Kim3

  • 1Department of Health Sciences and Technology, SAIHST, Sungkyunkwan University, Seoul, 06351, Republic of Korea.

Experimental & Molecular Medicine
|October 28, 2018
PubMed

Insights

The brain-expressed X-linked 4 (BEX4) gene interacts with Polo-like kinase 1 (PLK1), promoting cancer cell survival by enabling aneuploidy adaptation. This PLK1-BEX4 interaction offers a novel target for cancer therapy.

Area of Science:

  • Oncology
  • Molecular Biology
  • Cell Biology

Background:

  • Brain-expressed X-linked 4 (BEX4) is overexpressed in human cancers and linked to microtubule hyperacetylation via sirtuin 2 inhibition.
  • The precise molecular mechanism driving BEX4's oncogenic function in cancer remains incompletely understood.

Purpose of the Study:

  • To elucidate the gain-of-function molecular mechanism of the BEX4 gene in human cancers.
  • To investigate the interaction between BEX4 and Polo-like kinase 1 (PLK1) during mitosis.

Main Methods:

  • Immunofluorescence and co-immunoprecipitation assays to determine BEX4 and PLK1 localization and interaction.
  • Western blotting to assess protein stability following PLK1-mediated phosphorylation.

Main Results:

  • BEX4 and PLK1 were found to colocalize and interact at key mitotic structures, including centrosomes, spindle poles, and midbodies.
  • PLK1-mediated phosphorylation enhances BEX4 protein stability.
  • The PLK1-BEX4 interaction facilitates the adaptation of abnormal mitotic cells to aneuploidy, preventing apoptotic cell death.

Conclusions:

  • The oncogenicity of BEX4 is significantly driven by PLK1-mediated phosphorylation, stabilizing the BEX4 protein.
  • The BEX4-PLK1 interaction represents a novel oncogenic signaling pathway that promotes chromosomal aneuploidy acquisition in cancer cells.

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