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The MYC-associated protein CDCA7 is phosphorylated by AKT to regulate MYC-dependent apoptosis and transformation

R Montgomery Gill1, Timothy V Gabor, Amber L Couzens

  • 1Department of Biology, York University, Toronto, Ontario, Canada.

Molecular and Cellular Biology
|November 21, 2012
PubMed

Insights

Cell division control protein A7 (CDCA7) interacts with MYC, but AKT phosphorylation causes its release, affecting MYC-driven cell growth and apoptosis. This reveals a new pathway influencing cancer development.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Oncology

Background:

  • Cell division control protein A7 (CDCA7) is a MYC transcriptional target.
  • MYC is a key regulator of cell growth and transformation.
  • Understanding CDCA7's role in MYC signaling is crucial for cancer research.

Purpose of the Study:

  • To investigate the interaction between CDCA7 and MYC.
  • To elucidate the role of AKT phosphorylation in modulating CDCA7-MYC association.
  • To determine the functional impact of CDCA7 on MYC-dependent cellular processes.

Main Methods:

  • Co-immunoprecipitation to assess protein interactions.
  • Site-directed mutagenesis to study phosphorylation.
  • Cellular assays for apoptosis and fibroblast transformation.
  • Western blotting and immunofluorescence for protein localization.

Main Results:

  • CDCA7 directly associates with MYC.
  • AKT phosphorylates CDCA7 at Threonine 163, leading to 14-3-3 binding and cytoplasmic sequestration.
  • CDCA7 expression promotes MYC-dependent apoptosis and MYC-induced fibroblast transformation, while a non-interacting mutant inhibits it.

Conclusions:

  • AKT-mediated phosphorylation of CDCA7 disrupts its interaction with MYC.
  • This signaling pathway influences MYC's role in cell survival, apoptosis, and transformation.
  • The findings offer insights into a novel mechanism contributing to MYC-driven tumorigenesis.

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