ArticleFree radical biology & medicine2018
Methionine sulfoxide reductase A (MsrA) mediates the ubiquitination of 14-3-3 protein isotypes in brain.
Article in Free radical biology & medicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- A genome-wide interaction study of thyroid-stimulating hormone levels and particulate matter exposure among Koreans.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2026Article
- Methionine sulfoxide and the methionine sulfoxide reductase system as modulators of signal transduction pathways: a review.Amino acids · 2021Review
- Identification and confirmation of 14-3-3 ζ as a novel target of ginsenosides in brain tissues.Journal of ginseng research · 2021Article
- KRAS, YWHAE, SP1 and MSRA as biomarkers in endometrial cancer.Translational cancer research · 2021Article
- The Antioxidant Enzyme Methionine Sulfoxide Reductase A (MsrA) Interacts with Jab1/CSN5 and Regulates Its Function.Antioxidants (Basel, Switzerland) · 2020Article
- Oxyphylla A Promotes Degradation of α-Synuclein for NeuroprotectionAging and disease · 2020Article
- Akt Phosphorylates NQO1 and Triggers its Degradation, Abolishing Its Antioxidative Activities in Parkinson's Disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019Article
- Methionine Sulfoxide Reductases of Archaea.Antioxidants (Basel, Switzerland) · 2018Review
- The Functions of the Mammalian Methionine Sulfoxide Reductase System and Related Diseases.Antioxidants (Basel, Switzerland) · 2018Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
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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