Shapeshifting tau: from intrinsically disordered to paired-helical filaments.
Alzheimer's disease
amyloid
intrinsically disordered proteins
liquid liquid phase separation
protein misfolding
tau
Journal
Essays in biochemistry
ISSN: 1744-1358
Titre abrégé: Essays Biochem
Pays: England
ID NLM: 0043306
Informations de publication
Date de publication:
16 12 2022
16 12 2022
Historique:
received:
20
09
2022
revised:
25
10
2022
accepted:
26
10
2022
pubmed:
15
11
2022
medline:
20
12
2022
entrez:
14
11
2022
Statut:
ppublish
Résumé
Tau is an intrinsically disordered protein that has the ability to self-assemble to form paired helical and straight filaments in Alzheimer's disease, as well as the ability to form additional distinct tau filaments in other tauopathies. In the presence of microtubules, tau forms an elongated form associated with tubulin dimers via a series of imperfect repeats known as the microtubule binding repeats. Tau has recently been identified to have the ability to phase separate in vitro and in cells. The ability of tau to adopt a wide variety of conformations appears fundamental both to its biological function and also its association with neurodegenerative diseases. The recently highlighted involvement of low-complexity domains in liquid-liquid phase separation provides a critical link between the soluble function and the insoluble dysfunctional properties of tau.
Identifiants
pubmed: 36373666
pii: 232089
doi: 10.1042/EBC20220150
pmc: PMC9760425
doi:
Substances chimiques
tau Proteins
0
Tubulin
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1001-1011Informations de copyright
© 2022 The Author(s).
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