Abstract
The pathophysiology of Parkinson's disease, dementia with Lewy bodies, multiple system atrophy, and many others converge at alpha-synuclein (α-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 α-Syn aggregation and toxicity. These encompass distinct cellular strategies that tightly balance protein production, stability, and degradation, ultimately regulating α-Syn levels. Here, we review the main aspects of α-Syn biology, focusing on the cellular PQC components that are at the heart of recognizing and disposing toxic, aggregate-prone α-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 α-Syn aggregates.
Bidragets oversatte titel | protein kvalitets kontrolveje ved skilleveje for synukleinopatier |
---|---|
Originalsprog | Engelsk |
Tidsskrift | Journal of Parkinson's Disease |
Vol/bind | 10 |
Udgave nummer | 2 |
Sider (fra-til) | 369-382 |
Antal sider | 14 |
DOI | |
Status | Udgivet - 24 jan. 2020 |
Udgivet eksternt | Ja |
Emneord
- Sygdom, sundhedsvidenskab og sygepleje