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SUMO - a post-translational modification with therapeutic potential?

Journal

CURRENT OPINION IN PHARMACOLOGY
Volume 10, Issue 2, Pages 146-155

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.coph.2009.12.001

Keywords

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Funding

  1. American Heart Association [0625937T, SDG 0930360N]
  2. National Institute of Health [HL-088637, HL-064839, HL-077789]
  3. AHA [0740013N]
  4. NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL102746, R01HL064839, R01HL088637, P01HL077789] Funding Source: NIH RePORTER

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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.

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