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Regulation of p53 oligomerization by Ras superfamily protein RBEL1A

Ki Lui1, M Saeed Sheikh2, Ying Huang2

  • 1Department of Pharmacology, State University of New York, Upstate Medical University, Syracuse, NY, USA ; Division of Science and Technology, The Hong Kong Polytechnic University, Hong Kong Community College, Hung Hom, Kowloon, Hong Kong.

Genes & Cancer
|September 29, 2015
PubMed
Abstract

Insights

RBEL1A protein overexpression in tumors inhibits p53 oligomerization, impacting tumor cell growth. Silencing RBEL1A enhances p53 activity and target gene expression, revealing RBEL1A

Area of Science:

  • Molecular Biology
  • Oncology
  • Protein Interactions

Background:

  • RBEL1A is overexpressed in human malignancies.
  • RBEL1A interacts with the oligomeric domain of p53.
  • The effect of RBEL1A on p53 oligomerization and function was previously unknown.

Purpose of the Study:

  • To investigate the effect of RBEL1A on p53 oligomerization and function.
  • To elucidate the molecular mechanism by which RBEL1A regulates p53.

Main Methods:

  • In vitro oligomerization assays with purified RBEL1A and recombinant p53.
  • Cell-based assays to assess oligomerization of exogenous and endogenous p53.
  • RNA interference (RNAi) to silence RBEL1A expression.
  • Analysis of p53 target gene expression.

Main Results:

  • RBEL1A suppresses p53 oligomer formation in both unstressed and DNA-damaged cells.
  • The GTPase domain of RBEL1A (residues 1-235) is sufficient to block p53 oligomerization.
  • Silencing RBEL1A enhances p53 oligomeric complex formation and p53 target gene expression after DNA damage.

Conclusions:

  • RBEL1A negatively regulates p53 by inhibiting its tetramerization.
  • RBEL1A's oncogenic role is linked to its suppression of p53 function.
  • These findings provide molecular insights into p53 regulation and RBEL1A's role in malignancy.
Keywords:
RBEL1ARas superfamily GTPaseoligomerizationp53 tumor suppressor

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