Alpha-Synuclein is Involved in DYT1 Dystonia Striatal Synaptic Dysfunction.
SNAREs
asynchronous glutamate release
dystonia
striatum
synaptic vesicle turnover
α-synuclein
Journal
Movement disorders : official journal of the Movement Disorder Society
ISSN: 1531-8257
Titre abrégé: Mov Disord
Pays: United States
ID NLM: 8610688
Informations de publication
Date de publication:
05 2022
05 2022
Historique:
revised:
24
02
2022
received:
18
01
2022
accepted:
19
03
2022
pubmed:
15
4
2022
medline:
24
5
2022
entrez:
14
4
2022
Statut:
ppublish
Résumé
The neuronal protein alpha-synuclein (α-Syn) is crucially involved in Parkinson's disease pathophysiology. Intriguingly, torsinA (TA), the protein causative of DYT1 dystonia, has been found to accumulate in Lewy bodies and to interact with α-Syn. Both proteins act as molecular chaperones and control synaptic machinery. Despite such evidence, the role of α-Syn in dystonia has never been investigated. We explored whether α-Syn and N-ethylmaleimide sensitive fusion attachment protein receptor proteins (SNAREs), that are known to be modulated by α-Syn, may be involved in DYT1 dystonia synaptic dysfunction. We used electrophysiological and biochemical techniques to study synaptic alterations in the dorsal striatum of the Tor1a In the Tor1a Our data demonstrate an unprecedented relationship between TA and α-Syn, and reveal that α-Syn and SNAREs alterations characterize the synaptic dysfunction underlying DYT1 dystonia. © 2022 The Authors. Movement Disorders published by Wiley Periodicals LLC on behalf of International Parkinson Movement Disorder Society.
Sections du résumé
BACKGROUND
The neuronal protein alpha-synuclein (α-Syn) is crucially involved in Parkinson's disease pathophysiology. Intriguingly, torsinA (TA), the protein causative of DYT1 dystonia, has been found to accumulate in Lewy bodies and to interact with α-Syn. Both proteins act as molecular chaperones and control synaptic machinery. Despite such evidence, the role of α-Syn in dystonia has never been investigated.
OBJECTIVE
We explored whether α-Syn and N-ethylmaleimide sensitive fusion attachment protein receptor proteins (SNAREs), that are known to be modulated by α-Syn, may be involved in DYT1 dystonia synaptic dysfunction.
METHODS
We used electrophysiological and biochemical techniques to study synaptic alterations in the dorsal striatum of the Tor1a
RESULTS
In the Tor1a
CONCLUSIONS
Our data demonstrate an unprecedented relationship between TA and α-Syn, and reveal that α-Syn and SNAREs alterations characterize the synaptic dysfunction underlying DYT1 dystonia. © 2022 The Authors. Movement Disorders published by Wiley Periodicals LLC on behalf of International Parkinson Movement Disorder Society.
Identifiants
pubmed: 35420219
doi: 10.1002/mds.29024
pmc: PMC9323501
doi:
Substances chimiques
Dyt1 protein, mouse
0
Molecular Chaperones
0
SNARE Proteins
0
Snca protein, mouse
0
TOR1A protein, human
0
alpha-Synuclein
0
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
949-961Informations de copyright
© 2022 The Authors. Movement Disorders published by Wiley Periodicals LLC on behalf of International Parkinson Movement Disorder Society.
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