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 language | English |
|---|---|
| Title of host publication | International Review of Cell and Molecular Biology |
| Pages | 167-183 |
| Number of pages | 17 |
| DOIs | |
| State | Published - 2011 |
Publication series
| Name | International Review of Cell and Molecular Biology |
|---|---|
| Volume | 288 |
| 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
