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Journal Article

Folding of the Tau protein on microtubules.

MPS-Authors
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Kadavath,  H.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

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Jaremko,  M.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Jaremko,  L.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Kadavath, H., Jaremko, M., Jaremko, L., Biernat, J., Mandelkow, E., & Zweckstetter, M. (2015). Folding of the Tau protein on microtubules. Angewandte Chemie International Edition, 54(35), 10347-10351. doi:10.1002/anie.201501714.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0027-7D75-C
Abstract
Microtubules are regulated by microtubule-associated proteins. However, little is known about the structure of microtubule-associated proteins in complex with microtubules. Herein we show that the microtubule-associated protein Tau, which is intrinsically disordered in solution, locally folds into a stable structure upon binding to microtubules. While Tau is highly flexible in solution and adopts a β-sheet structure in amyloid fibrils, in complex with microtubules the conserved hexapeptides at the beginning of the Tau repeats two and three convert into a hairpin conformation. Thus, binding to microtubules stabilizes a unique conformation in Tau.