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- W3102152260 abstract "Abstract Tau is a microtubule-associated protein that regulates the stability of microtubules. We use metainference cryo-electron microscopy, an integrative structural biology approach, to determine an ensemble of structures representing the structure and dynamics of a tau-microtubule complex comprising the entire microtubule-binding region of tau. We thus identify the ground state of the complex and a series of excited states of lower populations. A comparison of the interactions in these different states reveals positions along the tau sequence that are important to determine the overall stability of the tau-microtubule complex. This analysis leads to the identification of positions where phosphorylation and acetylation events have destabilising effects, which we validate by using site-specific post-translationally modified tau variants obtained by chemical mutagenesis. Taken together, these results illustrate how the simultaneous determination of ground and excited states of macromolecular complexes reveals functional and regulatory mechanisms." @default.
- W3102152260 created "2020-11-23" @default.
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- W3102152260 date "2021-02-16" @default.
- W3102152260 modified "2023-09-25" @default.
- W3102152260 title "A structural ensemble of a tau-microtubule complex reveals regulatory tau phosphorylation and acetylation mechanisms" @default.
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- W3102152260 doi "https://doi.org/10.21203/rs.3.rs-215084/v1" @default.
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