dc.contributor.author | Oien, Derek B. | |
dc.contributor.author | Shinogle, Heather E. | |
dc.contributor.author | Moore, David S. | |
dc.contributor.author | Moskovitz, Jackob | |
dc.date.accessioned | 2017-05-24T17:02:34Z | |
dc.date.available | 2017-05-24T17:02:34Z | |
dc.date.issued | 2009-11 | |
dc.identifier.citation | Oien, 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. http://doi.org/10.1007/s12031-009-9274-8 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/24294 | |
dc.description.abstract | Aggregated 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.publisher | Humana Press | en_US |
dc.rights | © Humana Press 2009 | en_US |
dc.subject | Oxidative stress | en_US |
dc.subject | Posttranslation modification | en_US |
dc.subject | Neurodegenerative diseases | en_US |
dc.subject | Parkinson's disease | en_US |
dc.subject | Antioxidants | en_US |
dc.subject | Protein aggregation | en_US |
dc.subject | Yeast | en_US |
dc.subject | Synuclein | en_US |
dc.title | Clearance and Phosphorylation of Alpha-Synuclein Are Inhibited in Methionine Sulfoxide Reductase A Null Yeast Cells | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Oien, Derek B. | |
kusw.kuauthor | Shinogle, Heather E. | |
kusw.kuauthor | Moore, David S. | |
kusw.kuauthor | Moskovitz, Jackob | |
kusw.kudepartment | Pharmacology and Toxicology | en_US |
kusw.kudepartment | Pharmacy | en_US |
kusw.oanotes | Per SHERPA/RoMEO 5/24/2017: Author's Pre-print: green tick author can archive pre-print (ie pre-refereeing)
Author's Post-print: green tick author can archive post-print (ie final draft post-refereeing)
Publisher's Version/PDF: cross author cannot archive publisher's version/PDF
General Conditions: Author's pre-print on pre-print servers such as arXiv.org
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
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Articles in some journals can be made Open Access on payment of additional charge | en_US |
dc.identifier.doi | 10.1007/s12031-009-9274-8 | en_US |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC3708264 | en_US |
dc.rights.accessrights | openAccess | |