The DOI matches its Crossref record; 129 of the 129 references it cites were found in a registry or an index.
Implication of Alpha-Synuclein Phosphorylation at S129 in Synucleinopathies: What Have We Learned in the Last Decade?
Open accessAbstract
Abnormal accumulation of proteinaceous intraneuronal inclusions called Lewy bodies (LBs) is the neurpathological hallmark of Parkinson’s disease (PD) and related synucleinopathies. These inclusions are mainly constituted of a presynaptic protein, α-synuclein ( α-syn). Over the past decade, growing amounts of studies reported an aberrant accumulation of phosphorylated α-syn at the residue S129 (pS129) in the brain of patients suffering from PD, as well as in transgenic animal models of synucleinopathies. Whereas only a small fraction of α-syn (<4%) is phosphorylated in healthy brains, a dramatic accumulation of pS129 (>90%) has been observed within LBs, suggesting that this post-translational modification may play an important role in the regulation of α-syn aggregation, LBs formation and neuronal degeneration. However, whether phosphorylation at S129 suppresses or enhances α-syn aggregation and toxicity in vivo remains a subject of active debate. The answer to this question has important implications for understanding the role of phosphorylation in the pathogenesis of synucleinopathies and determining if targeting kinases or phosphatases could be a viable therapeutic strategy for the treatment of these devastating neurological disorders. In the present review, we explore recent findings from in vitro, cell-based assays and in vivo studies describing the potential implications of pS129 in the regulation of α-syn physiological functions, as well as its implication in synucleinopathies pathogenesis and diagnosis.
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3 retracted
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RetractedUbiquitination Increases Parkin Activity to Promote Autophagic α-Synuclein Clearance
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α-Synuclein is phosphorylated in synucleinopathy lesions
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α-Synuclein Promotes SNARE-Complex Assembly in Vivo and in Vitro
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Cited by
Impaired dopamine metabolism in Parkinson’s disease pathogenesis
Masato, A., Plotegher, N., Boassa, D., & Bubacco, L. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0332-6 · Cited by 328
Targeting Alpha-Synuclein as a Therapy for Parkinson’s Disease
Fields, C. R., Bengoa-Vergniory, N., & Wade-Martins, R. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00299 · Cited by 328
Grassi, D., Howard, S., Zhou, M., Diaz-Perez, N., Urban, N. T., Guerrero-Given, D., Kamasawa, N., Volpicelli-Daley, L. A., LoGrasso, P., & Lasmézas, C. I. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1713849115 · Cited by 228
Rey, N. L., George, S., Steiner, J. A., Madaj, Z., Luk, K. C., Trojanowski, J. Q., Lee, V. M.-Y., & Brundin, P. (2018) · Acta Neuropathologica · doi:10.1007/s00401-017-1792-9 · Cited by 215
Astrocytes have the capacity to act as antigen-presenting cells in the Parkinson’s disease brain
Rostami, J., Fotaki, G., Sirois, J., Mzezewa, R., Bergström, J., Essand, M., Healy, L., & Erlandsson, A. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01776-7 · Cited by 212
Metadata
- Authors
- Oueslati, A.
- Venue
- Journal of Parkinson’s Disease
- Publisher
- SAGE Publications
- Published
- 2016-03-11
- Volume
- 6
- Issue
- 1
- Pages
- 39-51
- ISSN
- 1877-7171 (ISSN-L)
- 1877-718X
- OpenAlex
- W2310305711
- Cited by
- 375
- References
- 129
- FWCI
- 18.67
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Oueslati, A. (2016). Implication of Alpha-Synuclein Phosphorylation at S129 in Synucleinopathies: What Have We Learned in the Last Decade? Journal of Parkinson’s Disease. https://doi.org/10.3233/jpd-160779
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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