Ubiquitin ligase TRIM71 suppresses ovarian tumorigenesis by degrading mutant p53

Cell Death Dis. 2019 Sep 30;10(10):737. doi: 10.1038/s41419-019-1977-3.

Abstract

Hotspot p53 mutants augment cancer cell proliferation, metastasis and metabolism through their gain-of-function (GOF). Ovarian cancer sustains the highest frequency of TP53 mutations, but the mechanisms underlying regulation of mutant p53s' GOF in this type of cancer remain incompletely understood. Herein, we identified the E3-ubiquitin ligase TRIM71 as a novel mutant p53-binding protein. Ectopic TRIM71-induced ubiquitination and proteasomal degradation of mutant p53 by binding to its transactivation (TA) domain, and inhibited the expression of a broad spectrum of mutant p53 target genes. Ectopic TRIM71 also restrained, whereas ablation of TRIM71 endorsed, ovarian carcinoma cell growth in vitro and in vivo. Significantly, TRIM71 overexpression is highly associated with favorable prognosis, particularly, in TP53-mutated ovarian carcinomas. Altogether, our findings unveil the anti-tumor function of TRIM71 in ovarian cancer development and prognosis by downregulating mutant p53s.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carcinogenesis / genetics*
  • Cell Line, Tumor
  • Databases, Genetic
  • Female
  • Gene Expression Regulation, Neoplastic / genetics
  • Heterografts
  • Humans
  • Male
  • Mice
  • Mutant Proteins / genetics
  • Ovarian Neoplasms / genetics*
  • Ovarian Neoplasms / pathology
  • Prostatic Neoplasms / genetics
  • Prostatic Neoplasms / pathology
  • Tripartite Motif Proteins / genetics*
  • Tumor Suppressor Protein p53 / genetics*
  • Ubiquitin-Protein Ligases / genetics*
  • Ubiquitination / genetics

Substances

  • Mutant Proteins
  • TP53 protein, human
  • Tripartite Motif Proteins
  • Tumor Suppressor Protein p53
  • TRIM71 protein, human
  • Ubiquitin-Protein Ligases