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dc.contributor.authorOien, Derek B.
dc.contributor.authorShinogle, Heather E.
dc.contributor.authorMoore, David S.
dc.contributor.authorMoskovitz, Jackob
dc.identifier.citationOien, D. B., Shinogle, H. E., Moore, D. S., & Moskovitz, J. (2009). Clearance and Phosphorylation of Alpha-Synuclein Are Inhibited in Methionine Sulfoxide Reductase A Null Yeast Cells. Journal of Molecular Neuroscience : MN, 39(3), 323–332.
dc.description.abstractAggregated α-synuclein and the point mutations Ala30Pro and Ala53Thr of α-synuclein are associated with Parkinson’s disease. The physiological roles of α-synuclein and methionine oxidation of the α-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 α-synuclein on basic cellular processes, α-synucleins were expressed in msrA null mutant and wild-type yeast cells. Protein degradation was inhibited in the α-synuclein-expressing msrA null mutant cells compared to α-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 α-synuclein phosphorylation in yeast cells and in vitro by casein kinase 2. Thus, a compromised MsrA function combined with α-synuclein overexpression may promote processes leading to synucleinopathies.en_US
dc.publisherHumana Pressen_US
dc.rights© Humana Press 2009en_US
dc.subjectOxidative stressen_US
dc.subjectPosttranslation modificationen_US
dc.subjectNeurodegenerative diseasesen_US
dc.subjectParkinson's diseaseen_US
dc.subjectProtein aggregationen_US
dc.titleClearance and Phosphorylation of Alpha-Synuclein Are Inhibited in Methionine Sulfoxide Reductase A Null Yeast Cellsen_US
kusw.kuauthorOien, Derek B.
kusw.kuauthorShinogle, Heather E.
kusw.kuauthorMoore, David S.
kusw.kuauthorMoskovitz, Jackob
kusw.kudepartmentPharmacology and Toxicologyen_US
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Author's pre-print on pre-print servers such as Author's post-print on author's personal website immediately Author's post-print on any open access repository after 12 months after publication Publisher's version/PDF cannot be used Published source must be acknowledged Must link to publisher version Set phrase to accompany link to published version (see policy) Articles in some journals can be made Open Access on payment of additional charge
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US

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