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Journal article
Methionine sulfoxide reductase A (MsrA) mediates the ubiquitination of 14-3-3 protein isotypes in brain
Free radical biology & medicine, v 129, pp 600-607
01 Dec 2018
PMID: 30096435
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The methionine sulfoxide reductase (Msr) system is known for its function in reducing protein-methionine sulfoxide to methionine. Recently, we showed that one member of the Msr system, MsrA, is involved in the ubiquitination-like process in Archaea. Here, the mammalian MsrA is demonstrated to mediate the ubiquitination of the 14-3-3 zeta protein and to promote the binding of 14-3-3 proteins to alpha synuclein in brain. MsrA was also found to enhance the ubiquitination and phosphorylation of Ser129 of alpha synuclein in brain. Furthermore, we demonstrate that, similarly to the archaeal MsrA, the mammalian MsrA can compete for capturing ubiquitin using the same active site it contains for methionine sulfoxide binding. Based on our previous observations showing that MsrA knockout mice have elevated expression levels of dopamine and 14-3-3 zeta and our current data, we propose that MsrA-dependent 14-3-3 zeta ubiquitination affects the regulation of alpha synuclein degradation and dopamine synthesis in the brain.
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Details
- Title
- Methionine sulfoxide reductase A (MsrA) mediates the ubiquitination of 14-3-3 protein isotypes in brain
- Creators
- Yue Deng - University of FloridaBeichen Jiang - University of FloridaCarolyn L. Rankin - University of FloridaKazuhito Toyo-oka - Drexel UniversityMark L. Richter - University of FloridaJulie A. Maupin-Furlow - Drexel UniversityJackob Moskovitz - Department of Microbiology and Cell Science, Institute of Food and Agricultural Sciences, University of Florida, Gainesville, FL 32611-0700, USA
- Publication Details
- Free radical biology & medicine, v 129, pp 600-607
- Publisher
- Elsevier
- Number of pages
- 8
- Grant note
- P30-AG-035982 / KU ADC Landon Center on Aging R01 GM57498 / NIH; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA R01GM057498 / NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of General Medical Sciences (NIGMS) Hedwig Miller Fund for Aging Research R01NS096098 / NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute of Neurological Disorders & Stroke (NINDS) P30AG035982 / NATIONAL INSTITUTE ON AGING; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Institute on Aging (NIA)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Neurobiology and Anatomy
- Web of Science ID
- WOS:000450298400055
- Scopus ID
- 2-s2.0-85051473588
- Other Identifier
- 991019168862804721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Endocrinology & Metabolism