Linking the Endoplasmic Reticulum to Parkinson’s Disease and Alpha-Synucleinopathy
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 neurodege...
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doaj-b0eb1b90d7914df48c73eb11634ab97a2020-11-25T01:45:00ZengFrontiers Media S.A.Frontiers in Neuroscience1662-453X2019-05-011310.3389/fnins.2019.00560461767Linking the Endoplasmic Reticulum to Parkinson’s Disease and Alpha-SynucleinopathyEmanuela CollaAccumulation 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 (αS), 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 αS can promote ER stress and cell death.https://www.frontiersin.org/article/10.3389/fnins.2019.00560/fullalpha-synucleinER stressUPRmisfolded proteinsParkinson’s diseasealpha-synucleinopathy |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Emanuela Colla |
spellingShingle |
Emanuela Colla Linking the Endoplasmic Reticulum to Parkinson’s Disease and Alpha-Synucleinopathy Frontiers in Neuroscience alpha-synuclein ER stress UPR misfolded proteins Parkinson’s disease alpha-synucleinopathy |
author_facet |
Emanuela Colla |
author_sort |
Emanuela Colla |
title |
Linking the Endoplasmic Reticulum to Parkinson’s Disease and Alpha-Synucleinopathy |
title_short |
Linking the Endoplasmic Reticulum to Parkinson’s Disease and Alpha-Synucleinopathy |
title_full |
Linking the Endoplasmic Reticulum to Parkinson’s Disease and Alpha-Synucleinopathy |
title_fullStr |
Linking the Endoplasmic Reticulum to Parkinson’s Disease and Alpha-Synucleinopathy |
title_full_unstemmed |
Linking the Endoplasmic Reticulum to Parkinson’s Disease and Alpha-Synucleinopathy |
title_sort |
linking the endoplasmic reticulum to parkinson’s disease and alpha-synucleinopathy |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Neuroscience |
issn |
1662-453X |
publishDate |
2019-05-01 |
description |
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 (αS), 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 αS can promote ER stress and cell death. |
topic |
alpha-synuclein ER stress UPR misfolded proteins Parkinson’s disease alpha-synucleinopathy |
url |
https://www.frontiersin.org/article/10.3389/fnins.2019.00560/full |
work_keys_str_mv |
AT emanuelacolla linkingtheendoplasmicreticulumtoparkinsonsdiseaseandalphasynucleinopathy |
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1725025950680219648 |