期刊
JOURNAL OF PARKINSONS DISEASE
卷 10, 期 2, 页码 369-382出版社
IOS PRESS
DOI: 10.3233/JPD-191790
关键词
Alpha-synuclein; synucleinopathies; protein homeostasis; protein aggregation; molecular chaperones; ubiquitin-proteasome system; autophagy
资金
- JPND - France, National Research Agency (ANR)
- Germany, Federal Ministry of Education and Research (BMBF)
- Netherlands, Netherlands Organization for Scientific Research (ZonMw)
- Sweden, Swedish Research Council (VR)
- Deutsche Forschungsgemeinschaft [SFB1036]
The pathophysiology of Parkinson's disease, dementia with Lewy bodies, multiple system atrophy, and many others converge at alpha-synuclein (alpha-Syn) aggregation. Although it is still not entirely clear what precise biophysical processes act as triggers, cumulative evidence points towards a crucial role for protein quality control (PQC) systems in modulating alpha-Syn aggregation and toxicity. These encompass distinct cellular strategies that tightly balance protein production, stability, and degradation, ultimately regulating alpha-Syn levels. Here, we review the main aspects of alpha-Syn biology, focusing on the cellular PQC components that are at the heart of recognizing and disposing toxic, aggregate-prone alpha-Syn assemblies: molecular chaperones and the ubiquitin-proteasome system and autophagy-lysosome pathway, respectively. A deeper understanding of these basic protein homeostasis mechanisms might contribute to the development of new therapeutic strategies envisioning the prevention and/or enhanced degradation of alpha-Syn aggregates.
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