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TY - JOUR AU - Tan, Ruensern AU - Lam, Aileen J. AU - Tan, Tracy AU - Han, Jisoo AU - Nowakowski, Dan W. AU - Vershinin, Michael AU - Simó, Sergi AU - Ori-McKenney, Kassandra M. AU - McKenney, Richard J. PY - 2019 DA - 2019/09/01 TI - Microtubules gate tau condensation to spatially regulate microtubule functions JO - Nature Cell Biology SP - 1078 EP - 1085 VL - 21 IS - 9 AB - 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. SN - 1476-4679 UR - https://doi.org/10.1038/s41556-019-0375-5 DO - 10.1038/s41556-019-0375-5 ID - Tan2019 ER -