SUMO-a post-translational modification with therapeutic potential?

Chang Hoon Woo, Jun-ichi Abe

Research output: Contribution to journalReview article

24 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)146-155
Number of pages10
JournalCurrent Opinion in Pharmacology
Volume10
Issue number2
DOIs
StatePublished - Apr 1 2010

Fingerprint

Sumoylation
Post Translational Protein Processing
Ubiquitin
Therapeutics
Cardiac Myocytes
Cardiovascular Diseases
Apoptosis
Peptides

ASJC Scopus subject areas

  • Drug Discovery
  • Pharmacology

Cite this

SUMO-a post-translational modification with therapeutic potential? / Woo, Chang Hoon; Abe, Jun-ichi.

In: Current Opinion in Pharmacology, Vol. 10, No. 2, 01.04.2010, p. 146-155.

Research output: Contribution to journalReview article

@article{54809750d5cd424ea559801a13ea66c7,
title = "SUMO-a post-translational modification with therapeutic potential?",
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.",
author = "Woo, {Chang Hoon} and Jun-ichi Abe",
year = "2010",
month = "4",
day = "1",
doi = "10.1016/j.coph.2009.12.001",
language = "English (US)",
volume = "10",
pages = "146--155",
journal = "Current Opinion in Pharmacology",
issn = "1471-4892",
publisher = "Elsevier BV",
number = "2",

}

TY - JOUR

T1 - SUMO-a post-translational modification with therapeutic potential?

AU - Woo, Chang Hoon

AU - Abe, Jun-ichi

PY - 2010/4/1

Y1 - 2010/4/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=77949725836&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77949725836&partnerID=8YFLogxK

U2 - 10.1016/j.coph.2009.12.001

DO - 10.1016/j.coph.2009.12.001

M3 - Review article

C2 - 20079693

AN - SCOPUS:77949725836

VL - 10

SP - 146

EP - 155

JO - Current Opinion in Pharmacology

JF - Current Opinion in Pharmacology

SN - 1471-4892

IS - 2

ER -