Tau accelerates tubulin exchange in the microtubule lattice

Abstract Microtubules are cytoskeletal filaments characterized by dynamic instability at their tips and a dynamic lattice that undergoes continuous tubulin loss and incorporation. Tau, a neuronal microtubule-associated protein, is well known for its role in stabilizing microtubule tips and promoting microtubule bundling. Here we demonstrate that tau also modulates microtubule lattice dynamics. Although tau lacks enzymatic activity, it significantly accelerates tubulin exchange within the lattice, particularly at topological defect sites. Our findings indicate that tau enhances lattice anisotropy by stabilizing longitudinal tubulin–tubulin interactions while destabilizing lateral ones, thereby enhancing the mobility and annihilation of lattice defects. These results challenge the traditional view of tau as merely a passive stabilizer, revealing its active role in dynamically remodelling the microtubule lattice structure.

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Publication Details

Journal
Nature Physics
Published
2025-09-04
DOI
https://doi.org/10.1038/s41567-025-03003-7
Citations
2
Primary Topic
Microtubule and mitosis dynamics
Type
article
Field-Weighted Citation Impact
2.30

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article

Tau accelerates tubulin exchange in the microtubule lattice

Stefan Diez, Laura Schaedel, Cordula Reuther, Chetan Poojari et al.
2 citations
Nature Physics
Microtubule and mitosis dynamics
2.30
article

Tau accelerates tubulin exchange in the microtubule lattice

Stefan Diez, Laura Schaedel, Cordula Reuther, Chetan Poojari, Karin John, Subhadra Nandakumar, Jochen S. Hub, M. Reza Shaebani, Rahul Grover, Amir Zablotsky, Subham Biswas, Mona Grünewald
article en
2 citations

Abstract

Abstract Microtubules are cytoskeletal filaments characterized by dynamic instability at their tips and a dynamic lattice that undergoes continuous tubulin loss and incorporation. Tau, a neuronal microtubule-associated protein, is well known for its role in stabilizing microtubule tips and promoting microtubule bundling. Here we demonstrate that tau also modulates microtubule lattice dynamics. Although tau lacks enzymatic activity, it significantly accelerates tubulin exchange within the lattice, particularly at topological defect sites. Our findings indicate that tau enhances lattice anisotropy by stabilizing longitudinal tubulin–tubulin interactions while destabilizing lateral ones, thereby enhancing the mobility and annihilation of lattice defects. These results challenge the traditional view of tau as merely a passive stabilizer, revealing its active role in dynamically remodelling the microtubule lattice structure.

Nature PhysicsVol. 21(10)
Centre National de la Recherche Scientifique (FR), Laboratoire Interdisciplinaire de Physique (FR), Institut für Sozialforschung und Sozialwirtschaft (DE), Center for Systems Biology Dresden (DE), Max Planck Institute of Molecular Cell Biology and Genetics (DE), Technische Universität Dresden (DE), Université Grenoble Alpes (FR), Saarland University (DE)
Deutsche Forschungsgemeinschaft, Technische Universität Dresden, Universität des Saarlandes
Openalex Percentile: Top 11%
Microtubule and mitosis dynamics
2.30
DOIOpen Access PDFOpenAlex
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