SUMO--a post-translational modification with therapeutic potential?
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.
Woo
Chang-Hoon
CH
Aab Cardiovascular Research Institute, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Box CVRI, Rochester, NY 14642, United States.
Abe
Jun-Ichi
J
D000818:Animals; D002318:Cardiovascular Diseases / Q000188:drug therapy / Q000378:metabolism*; D002319:Cardiovascular System / Q000378:metabolism*; D003925:Diabetic Angiopathies / Q000378:metabolism; D016503:Drug Delivery Systems / Q000379:methods*; D006801:Humans; D008954:Models, Biological; D020641:Polymorphism, Single Nucleotide; D011499:Protein Processing, Post-Translational; D025841:Small Ubiquitin-Related Modifier Proteins / Q000235:genetics / Q000378:metabolism*
D025841:Small Ubiquitin-Related Modifier Proteins