Identification of the three zinc-binding sites on tau protein - Archive ouverte HAL Access content directly
Journal Articles International Journal of Biological Macromolecules Year : 2022

Identification of the three zinc-binding sites on tau protein

Romain Rocca
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Andrey Golovin
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Diane Allegro
Pascale Barbier
Soazig Malesinski
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François Devred


Tau protein has been extensively studied due to its key roles in microtubular cytoskeleton regulation and in the formation of aggregates found in some neurodegenerative diseases. Recently it has been shown that zinc is able to induce tau aggregation by interacting with several binding sites. However, the precise location of these sites and the molecular mechanism of zinc-induced aggregation remain unknown. Here we used Nuclear Magnetic Resonance (NMR) to identify zinc binding sites on tau. These experiments revealed three distinct zinc binding sites on tau, located in the N-terminal part, the repeat region and the C-terminal part. Further analysis enabled us to show that the N-terminal and the C-terminal sites are independent of each other. Using molecular simulations, we proposed a model of each site in a complex with zinc. Given the clinical importance of zinc in tau aggregation, our findings pave the way for designing potential therapies for tauopathies.


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hal-03647684 , version 1 (29-04-2022)



Romain Rocca, Philipp O Tsvetkov, Andrey Golovin, Diane Allegro, Pascale Barbier, et al.. Identification of the three zinc-binding sites on tau protein. International Journal of Biological Macromolecules, 2022, 209, pp.779-784. ⟨10.1016/j.ijbiomac.2022.04.058⟩. ⟨hal-03647684⟩
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