Microtubules gate tau condensation to spatially regulate microtubule functions.
Nat Cell Biol
; 21(9): 1078-1085, 2019 09.
Article
em En
| MEDLINE
| ID: mdl-31481790
ABSTRACT
Tau is an abundant microtubule-associated protein in neurons. Tau aggregation into insoluble fibrils is a hallmark of Alzheimer's disease and other types of dementia1, yet the physiological state of tau molecules within cells remains unclear. Using single-molecule imaging, we directly observe that the microtubule lattice regulates reversible tau self-association, leading to localized, dynamic condensation of tau molecules on the microtubule surface. Tau condensates form selectively permissible barriers, spatially regulating the activity of microtubule-severing enzymes and the movement of molecular motors through their boundaries. We propose that reversible self-association of tau molecules, gated by the microtubule lattice, is an important mechanism of the biological functions of tau, and that oligomerization of tau is a common property shared between the physiological and disease-associated forms of the molecule.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas tau
/
Espastina
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Proteínas Associadas aos Microtúbulos
/
Microtúbulos
Limite:
Animals
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article