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Publication / Research
On October 4, 2025

An interdisciplinary team of researchers from Germany and the LIPhy has demonstrated that Tau, a neuronal protein known for stabilizing microtubule tips, plays an active role in modulating microtubule lattice dynamics. The study reveals that Tau significantly accelerates the exchange of tubulin within the microtubule lattice, especially at topological defect sites, despite lacking enzymatic activity. These findings challenge the traditional view of Tau as merely a passive stabilizer, showing instead that it increases lattice anisotropy and, in doing so, actively enhances microtubule lattice dynamics.
To find out more, take a look at the scientific article published in Nature Physics.
Date
Contact
Karin JOHN
karin.johnuniv-grenoble-alpes.fr (karin[dot]john[at]univ-grenoble-alpes[dot]fr)
Reference
S. Biswas, R. Grover, C. Reuther, C. S. Poojari, R. Shaebani, S. Nandakumar, M. Grünewald, A. Zablotsky, J. S. Hub, S. Diez, K. John & L. Schaedel. Tau accelerates tubulin exchange in the microtubule lattice. Nat. Phys. 1745-2481 (2025)
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