AI Article Synopsis
- SUMO polypeptide attachment (sumoylation) is a key regulator for many proteins linked to human diseases, such as various neurodegenerative disorders and cancer.
- Two recent studies have identified that amyloid precursor protein (APP) and lamin A are also sumoylated, which may help in understanding their roles in diseases like Alzheimer's and familial dilated cardiomyopathy.
- APP sumoylation appears to influence Aβ peptide levels related to Alzheimer's, while mutations affecting lamin A sumoylation have been linked to specific heart conditions.
Article 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.
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| http://dx.doi.org/10.1016/B978-0-12-386041-5.00004-2 | DOI Listing |
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