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Trends Biochem Sci. 2009 Apr;34(4):200-5. doi: 10.1016/j.tibs.2009.01.004. Epub 2009 Mar 11.

Sumoylation and human disease pathogenesis.

Author information

1
Department of Molecular and Cellular Biochemistry, Chandler Medical Center, University of Kentucky, Lexington, KY 40536, USA. kdsarge@uky.edu

Abstract

Covalent modification by SUMO polypeptides, or sumoylation, is an important regulator of the functional properties of many proteins. Among these are several proteins implicated in human diseases including cancer, Huntington's, Alzheimer's, and Parkinson's diseases, as well as spinocerebellar ataxia 1 and amyotrophic lateral sclerosis. Recent reports reveal two new examples of human disease-associated proteins that are SUMO modified: amyloid precursor protein and lamin A. These findings point to a function for sumoylation in modulating amyloid-beta peptide levels, indicating a potential role in Alzheimer's disease, and for decreased lamin A sumoylation as a causative factor in familial dilated cardiomyopathy.

PMID:
19282183
PMCID:
PMC2974900
DOI:
10.1016/j.tibs.2009.01.004
[Indexed for MEDLINE]
Free PMC Article

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