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Purification of Ubiquitinated p53 Proteins from Mammalian Cells
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Ubiquitin ligase TRIM71 suppresses ovarian tumorigenesis by degrading mutant p53

Yajie Chen1,2,3, Qian Hao1,3, Jieqiong Wang1,3

  • 1Cancer Institute, Fudan University Shanghai Cancer Center, Fudan University, Shanghai, 200032, China.

Cell Death & Disease
|October 2, 2019
PubMed

Insights

Researchers found TRIM71, an E3-ubiquitin ligase, targets mutant p53 in ovarian cancer. TRIM71 reduces tumor growth and is linked to better patient outcomes, revealing its anti-cancer role.

Area of Science:

  • Oncology
  • Molecular Biology
  • Biochemistry

Background:

  • Hotspot p53 mutants promote cancer progression via gain-of-function (GOF).
  • Ovarian cancer frequently harbors TP53 mutations, yet regulation of mutant p53 GOF is not fully understood.

Purpose of the Study:

  • To identify novel regulators of mutant p53 gain-of-function in ovarian cancer.
  • To investigate the role of TRIM71 in mutant p53 regulation and ovarian cancer progression.

Main Methods:

  • Identified TRIM71 as a direct binding partner of mutant p53.
  • Demonstrated TRIM71-induced ubiquitination and proteasomal degradation of mutant p53.
  • Assessed the impact of TRIM71 modulation on ovarian carcinoma cell growth in vitro and in vivo.

Main Results:

  • TRIM71 binds to the transactivation domain of mutant p53, promoting its degradation.
  • Ectopic TRIM71 expression inhibited ovarian carcinoma cell proliferation and tumor growth.
  • TRIM71 ablation accelerated tumor progression.
  • TRIM71 overexpression correlated with favorable prognosis in TP53-mutated ovarian cancers.

Conclusions:

  • TRIM71 functions as an anti-tumor factor in ovarian cancer by downregulating mutant p53.
  • TRIM71 represents a potential therapeutic target for improving prognosis in TP53-mutated ovarian cancers.

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