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Olig2 SUMOylation protects against genotoxic damage response by antagonizing p53 gene targeting

Huiqing Liu1, Weiji Weng1, Rongjun Guo1,2

  • 1Department of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine, Shanghai, 200025, China.

Cell Death and Differentiation
|June 3, 2020
PubMed

Insights

Small ubiquitin-like modifier-1 (SUMO1) conjugation of oligodendrocyte transcription factor 2 (Olig2) is crucial for glioma resistance to genotoxic drugs. SUMOylation and phosphorylation of Olig2 suppress apoptosis and enhance cancer survival.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Epigenetics

Background:

  • Posttranslational modifications (PTMs) of nuclear proteins are critical in cancer.
  • Oligodendrocyte transcription factor 2 (Olig2) phosphorylation is implicated in glioma drug resistance, but mechanisms are unclear.

Purpose of the Study:

  • To investigate the role of Olig2 SUMOylation in glioma resistance to genotoxic agents.
  • To elucidate the interplay between Olig2 SUMOylation and phosphorylation in regulating cancer cell survival.

Main Methods:

  • Western blotting to detect Olig2 SUMOylation and phosphorylation.
  • Cell-based assays to assess Olig2's role in cell cycle arrest and apoptosis.
  • Chromatin immunoprecipitation to evaluate p53 binding to the Cdkn1a promoter.

Main Results:

  • Olig2 is SUMOylated at lysine residues K27, K76, and K112.
  • SUMOylation, along with TSM phosphorylation, is essential for Olig2's antiapoptotic function.
  • Olig2 SUMOylation suppresses p53-mediated cell cycle arrest and apoptosis, conferring resistance to temozolomide (TMZ).
  • SUMOylated Olig2 inhibits p53 recruitment to the Cdkn1a promoter, impairing DNA damage response.

Conclusions:

  • Olig2 SUMOylation is a novel regulatory mechanism controlling glioma cell survival.
  • Targeting Olig2 SUMOylation may offer a therapeutic strategy for overcoming chemoresistance in gliomas.

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