Role of aberrant phase separation in pathological protein aggregation.
Journal
Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784
Informations de publication
Date de publication:
10 2023
10 2023
Historique:
received:
08
06
2023
revised:
13
07
2023
accepted:
17
07
2023
medline:
18
9
2023
pubmed:
22
8
2023
entrez:
21
8
2023
Statut:
ppublish
Résumé
Neurodegenerative diseases are associated with the pathological deposition of many different intrinsically disordered proteins or proteins with intrinsically disordered regions. Recent evidence suggests that these proteins can undergo liquid-liquid phase separation and also form membrane-less organelles in cells. Additionally, the biomolecular condensates formed by these proteins may undergo liquid-to-solid phase transition thereby maturating to amyloid fibrils, oligomeric species, or amorphous aggregates and contributing to the pathology of several neurodegenerative diseases. Here we discuss the role of phase separation of the neuronal proteins tau, α-synuclein, fused in sarcoma (FUS), and the transactive response DNA-binding protein of 43 kDa (TDP-43) that are associated with neurodegeneration in the context of pathological protein aggregation.
Identifiants
pubmed: 37604044
pii: S0959-440X(23)00152-5
doi: 10.1016/j.sbi.2023.102678
pii:
doi:
Substances chimiques
Intrinsically Disordered Proteins
0
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
102678Informations de copyright
Copyright © 2023 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare no competing financial interests.