Cancer-Associated Dysregulation of Sumo Regulators: Proteases and Ligases

Int J Mol Sci. 2022 Jul 20;23(14):8012. doi: 10.3390/ijms23148012.

Abstract

SUMOylation is a post-translational modification that has emerged in recent decades as a mechanism involved in controlling diverse physiological processes and that is essential in vertebrates. The SUMO pathway is regulated by several enzymes, proteases and ligases being the main actors involved in the control of sumoylation of specific targets. Dysregulation of the expression, localization and function of these enzymes produces physiological changes that can lead to the appearance of different types of cancer, depending on the enzymes and target proteins involved. Among the most studied proteases and ligases, those of the SENP and PIAS families stand out, respectively. While the proteases involved in this pathway have specific SUMO activity, the ligases may have additional functions unrelated to sumoylation, which makes it more difficult to study their SUMO-associated role in cancer process. In this review we update the knowledge and advances in relation to the impact of dysregulation of SUMO proteases and ligases in cancer initiation and progression.

Keywords: SUMO; cancer; ligase; protease; regulation; transcription.

Publication types

  • Review

MeSH terms

  • Animals
  • Endopeptidases / metabolism
  • Humans
  • Ligases* / metabolism
  • Neoplasms*
  • Peptide Hydrolases / metabolism
  • Protein Processing, Post-Translational
  • Small Ubiquitin-Related Modifier Proteins / metabolism
  • Sumoylation
  • Ubiquitin-Protein Ligases / metabolism

Substances

  • Small Ubiquitin-Related Modifier Proteins
  • Ubiquitin-Protein Ligases
  • Endopeptidases
  • Peptide Hydrolases
  • Ligases