SUMO and Its Role in Human Diseases

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

70 Scopus citations

Abstract

The covalent attachment of small ubiquition-like modifier (SUMO) polypeptides, or sumoylation, is an important regulator of the functional properties of many proteins. Among these are many proteins implicated in human diseases including cancer and Huntington's, Alzheimer's, and Parkinson's diseases, as well as spinocerebellar ataxia 1 and amyotrophic lateral sclerosis. The results of two more recent studies identify two additional human disease-associated proteins that are sumoylated, amyloid precursor protein (APP), and lamin A. APP sumoylation modulates Aβ peptide levels, suggesting a potential role in Alzheimer's disease, and decreased lamin A sumoylation due to mutations near its SUMO site has been implicated in causing some forms of familial dilated cardiomyopathy.

Original languageEnglish
Title of host publicationInternational Review of Cell and Molecular Biology
Pages167-183
Number of pages17
DOIs
StatePublished - 2011

Publication series

NameInternational Review of Cell and Molecular Biology
Volume288
ISSN (Print)1937-6448

Bibliographical note

Funding Information:
The authors acknowledge the support of NIH grants GM61053 and GM64606 to K. D. S., which enabled us to perform our studies cited in this review.

Keywords

  • ALS
  • APP
  • Alzheimer's disease
  • Amyotrophic lateral sclerosis
  • Cancer
  • DJ-1
  • Heart
  • Lamin
  • Laminopathy
  • Parkinson's disease
  • SOD1
  • SUMO
  • SUMO-1
  • Sumoylation
  • Tau
  • α-Synuclein

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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