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Nat Cell Biol. 2019 Sep;21(9):1078-1085. doi: 10.1038/s41556-019-0375-5. Epub 2019 Sep 2.

Microtubules gate tau condensation to spatially regulate microtubule functions.

Author information

1
Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA, USA.
2
Department of Cell Biology and Human Anatomy, School of Medicine, University of California, Davis, Davis, CA, USA.
3
N Molecular Systems, Inc., Palo Alto, CA, USA.
4
Department of Physics & Astronomy, University of Utah, Salt Lake City, UT, USA.
5
Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA, USA. kmorimckenney@ucdavis.edu.
6
Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA, USA. rjmckenney@ucdavis.edu.

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.

PMID:
31481790
PMCID:
PMC6748660
[Available on 2020-03-02]
DOI:
10.1038/s41556-019-0375-5

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