Microtubules gate tau condensation to spatially regulate microtubule functions.

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.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Tan R,Lam AJ,Tan T,Han J,Nowakowski DW,Vershinin M,Simó S,Ori-McKenney KM,McKenney RJ

doi

10.1038/s41556-019-0375-5

subject

Has Abstract

pub_date

2019-09-01 00:00:00

pages

1078-1085

issue

9

eissn

1465-7392

issn

1476-4679

pii

10.1038/s41556-019-0375-5

journal_volume

21

pub_type

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