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Coiled-coil domain containing 85B suppresses the beta-catenin activity in a p53-dependent manner

A Iwai1, M Hijikata, T Hishiki

  • 1Division of Gastroenterology and Hepatology, Department of Medicine, Kyoto University, Kyoto, Japan.

Oncogene
|September 18, 2007
PubMed

Insights

p53-induced CCDC85B protein degrades beta-catenin, independent of GSK3beta, suppressing tumor growth. This reveals a novel p53 pathway regulating beta-catenin activity in cancer.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Cell Biology

Background:

  • Aberrant beta-catenin accumulation is a hallmark of carcinogenesis.
  • p53 gene mutations can lead to beta-catenin accumulation independently of the GSK3beta pathway, but the mechanism is unclear.

Purpose of the Study:

  • To investigate the role of human coiled-coil domain containing 85B (CCDC85B) in regulating beta-catenin activity.
  • To elucidate the mechanism by which p53 influences beta-catenin levels.

Main Methods:

  • Investigated the interaction between CCDC85B and T-cell factor 4 (TCF4) in the nucleus.
  • Assessed the effect of CCDC85B on beta-catenin degradation.
  • Evaluated the impact of CCDC85B on tumor cell growth.

Main Results:

  • CCDC85B is induced by p53.
  • CCDC85B interacts with TCF4 in the nucleus, regulating beta-catenin.
  • CCDC85B enhances beta-catenin degradation and suppresses tumor cell proliferation.
  • CCDC85B-mediated beta-catenin degradation is independent of GSK3beta and Siah-1L.

Conclusions:

  • CCDC85B is a novel p53-inducible protein that regulates beta-catenin.
  • CCDC85B promotes beta-catenin degradation through a GSK3beta-independent mechanism.
  • CCDC85B represents a component of p53-mediated regulatory pathways controlling beta-catenin in cancer development.

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