학술논문
Microtubules gate tau condensation to spatially regulate microtubule functions
Document Type
Report
Author
Source
Nature Cell Biology. September 2019, Vol. 21 Issue 9, 1078
Subject
Language
English
ISSN
1465-7392
Abstract
Author(s): Ruensern Tan [sup.1] , Aileen J. Lam [sup.1] , Tracy Tan [sup.1] , Jisoo Han [sup.2] , Dan W. Nowakowski [sup.3] , Michael Vershinin [sup.4] , Sergi Simó [sup.2] [...]
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 dementia.sup.1, 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. Tan et al. and Siahaan et al. present distinct but complementary data showing that microtubule regulates dynamic condensation of tau molecules, and this in turn affects microtubule biology and function.
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 dementia.sup.1, 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. Tan et al. and Siahaan et al. present distinct but complementary data showing that microtubule regulates dynamic condensation of tau molecules, and this in turn affects microtubule biology and function.