SUMO--a post-translational modification with therapeutic potential?

Curr Opin Pharmacol. 2010 Apr;10(2):146-55. doi: 10.1016/j.coph.2009.12.001. Epub 2010 Jan 14.

Abstract

Sumoylation is a covalent modification, which is mediated by small ubiquitin-like modifier (SUMO) polypeptides. A growing body of evidence has shown that sumoylation affects the functional properties of many substrates in the regulation of cellular processes. Recent reports indicate the crucial role of sumoylation in human diseases including familial dilated cardiomyopathy, suggesting that targeting of sumoylation would be of considerable interest for novel therapies. Even though hundreds of SUMO substrates have been identified, their pathophysiological roles remain to be determined. Among them, ERK5-sumoylation has recently been linked to diabetes and implicated in endothelial dysfunction and cardiomyocyte apoptosis in vivo. These findings support the idea that ERK5-sumoylation is a novel therapeutic target for the treatment of diabetes-related cardiovascular diseases.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cardiovascular Diseases / drug therapy
  • Cardiovascular Diseases / metabolism*
  • Cardiovascular System / metabolism*
  • Diabetic Angiopathies / metabolism
  • Drug Delivery Systems / methods*
  • Humans
  • Models, Biological
  • Polymorphism, Single Nucleotide
  • Protein Processing, Post-Translational*
  • Small Ubiquitin-Related Modifier Proteins / genetics
  • Small Ubiquitin-Related Modifier Proteins / metabolism*

Substances

  • Small Ubiquitin-Related Modifier Proteins