Microtubules gate tau condensation to spatially regulate microtubule functions

Ruensern Tan, Aileen J. Lam, Tracy Tan, Jisoo Han, Dan W. Nowakowski, Michael Vershinin, Sergi Simó, Kassandra M. Ori-McKenney, Richard J. McKenney

Research output: Contribution to journalLetterpeer-review

60 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1078-1085
Number of pages8
JournalNature Cell Biology
Issue number9
StatePublished - Sep 1 2019

ASJC Scopus subject areas

  • Cell Biology


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