Journal
JOURNAL OF MOLECULAR NEUROSCIENCE
Volume 39, Issue 3, Pages 323-332Publisher
HUMANA PRESS INC
DOI: 10.1007/s12031-009-9274-8
Keywords
Oxidative stress; Posttranslation modification; Neurodegenerative diseases; Parkinson's disease; Antioxidants; Protein aggregation; Yeast; Synuclein
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Funding
- Kansas EPSCOR/National Science Foundation
- National Institute of Aging [AG027363]
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Aggregated a-synuclein and the point mutations A1a30Pro and A1a53Thr of alpha-synuclein are associated with Parkinson's disease. The physiological roles of alpha-synuclein and methionine oxidation of the alpha-synuclein protein structure and function are not fully understood. Methionine sulfoxide reductase A (MsrA) reduces methionine sulfoxide residues and functions as an antioxidant. To monitor the effect of methionine oxidation to alpha-synuclein on basic cellular processes, alpha-synucleins were expressed in msrA null mutant and wild-type yeast cells. Protein degradation was inhibited in the alpha-synuclein-expressing msrA null mutant cells compared to alpha-synuclein-expressing wild-type cells. Increased inhibition of degradation and elevated accumulations of fibrillated proteins were observed in SynA30P-expressing msrA null mutant cells. Additionally, methionine oxidation inhibited alpha-synuclein phosphorylation in yeast cells and in vitro by casein kinase 2. Thus, a compromised MsrA function combined with alpha-synuclein overexpression may promote processes leading to synucleinopathies.
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