Structural polymorphism of the low-complexity C-terminal domain of TDP-43 amyloid aggregates revealed by solid-state NMR.
TDP-43
amyloid
amyotrophic lateral sclerosis
frontotemporal dementia
low-complexity domain
polymorphism
solid-state NMR
Journal
Frontiers in molecular biosciences
ISSN: 2296-889X
Titre abrégé: Front Mol Biosci
Pays: Switzerland
ID NLM: 101653173
Informations de publication
Date de publication:
2023
2023
Historique:
received:
19
01
2023
accepted:
17
03
2023
medline:
18
4
2023
entrez:
17
4
2023
pubmed:
18
4
2023
Statut:
epublish
Résumé
Aberrant aggregation of the transactive response DNA-binding protein (TDP-43) is associated with several lethal neurodegenerative diseases, including amyotrophic lateral sclerosis and frontotemporal dementia. Cytoplasmic neuronal inclusions of TDP-43 are enriched in various fragments of the low-complexity C-terminal domain and are associated with different neurotoxicity. Here we dissect the structural basis of TDP-43 polymorphism using magic-angle spinning solid-state NMR spectroscopy in combination with electron microscopy and Fourier-transform infrared spectroscopy. We demonstrate that various low-complexity C-terminal fragments, namely TDP-13 (TDP-43
Identifiants
pubmed: 37065450
doi: 10.3389/fmolb.2023.1148302
pii: 1148302
pmc: PMC10095165
doi:
Types de publication
Journal Article
Langues
eng
Pagination
1148302Informations de copyright
Copyright © 2023 Shenoy, Lends, Berbon, Bilal, El Mammeri, Bertoni, Saad, Morvan, Grélard, Lecomte, Theillet, Buell, Kauffmann, Habenstein and Loquet.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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