Journal
FRONTIERS IN NEUROSCIENCE
Volume 13, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fnins.2019.00560
Keywords
alpha-synuclein; ER stress; UPR; misfolded proteins; Parkinson's disease; alpha-synucleinopathy; alpha-synuclein aggregates
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Funding
- Italian Ministry of University and Research (MIUR), Career Reintegration Grant scheme (RLM Program for Young Researchers)
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Accumulation of misfolded proteins is a central paradigm in neurodegeneration. Because of the key role of the endoplasmic reticulum (ER) in regulating protein homeostasis, in the last decade multiple reports implicated this organelle in the progression of Parkinson's Disease (PD) and other neurodegenerative illnesses. In PD, dopaminergic neuron loss or more broadly neurodegeneration has been improved by overexpression of genes involved in the ER stress response. In addition, toxic alpha-synuclein (alpha S), the main constituent of proteinaceous aggregates found in tissue samples of PD patients, has been shown to cause ER stress by altering intracellular protein traffic, synaptic vesicles transport, and Ca2+ homeostasis. In this review, we will be summarizing evidence correlating impaired ER functionality to PD pathogenesis, focusing our attention on how toxic, aggregated alpha S can promote ER stress and cell death.
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