Novel compounds that synergize with aminoglycoside G418 or eRF3 degraders for translational readthrough of nonsense mutant TP53 and PTEN

RNA Biol. 2023 Jan;20(1):368-383. doi: 10.1080/15476286.2023.2222250.

Abstract

The TP53 and PTEN tumour suppressor genes are inactivated by nonsense mutations in a significant fraction of human tumours. TP53 nonsense mutatant tumours account for approximately one million new cancer cases per year worldwide. We have screened chemical libraries with the aim of identifying compounds that induce translational readthrough and expression of full-length p53 protein in cells with nonsense mutation in this gene. Here we describe two novel compounds with readthrough activity, either alone or in combination with other known readthrough-promoting substances. Both compounds induced levels of full-length p53 in cells carrying R213X nonsense mutant TP53. Compound C47 showed synergy with the aminoglycoside antibiotic and known readthrough inducer G418, whereas compound C61 synergized with eukaryotic release factor 3 (eRF3) degraders CC-885 and CC-90009. C47 alone showed potent induction of full-length PTEN protein in cells with different PTEN nonsense mutations. These results may facilitate further development of novel targeted cancer therapy by pharmacological induction of translational readthrough.

Keywords: PTEN; TP53; nonsense mutation; novel compounds; synergy; translational readthrough.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aminoglycosides* / pharmacology
  • Anti-Bacterial Agents / pharmacology
  • Codon, Nonsense
  • Humans
  • Neoplasms*
  • PTEN Phosphohydrolase / genetics
  • PTEN Phosphohydrolase / metabolism
  • Protein Synthesis Inhibitors
  • Tumor Suppressor Protein p53 / genetics
  • Tumor Suppressor Protein p53 / metabolism

Substances

  • Aminoglycosides
  • antibiotic G 418
  • peptide-chain-release factor 3
  • Codon, Nonsense
  • Tumor Suppressor Protein p53
  • PTEN Phosphohydrolase
  • Anti-Bacterial Agents
  • Protein Synthesis Inhibitors
  • TP53 protein, human
  • PTEN protein, human

Grants and funding

The work was supported by the Barncancerfonden [Barncancerfonden PR2020-0042]; Cancerfonden [Cancerfonden 18 0774; 21 1473 Pj 01 H]; European Research Council [No. 694825-TRANSREAD]; Olga Jönssons Stiftelse, Uppsala University; Vetenskapsrådet [VR 2017-01509; 2021-02064] and Karolinska Institutet