Folding of the Tau Protein on Microtubules
2015 | journal article. A publication with affiliation to the University of Göttingen.
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Folding of the Tau Protein on Microtubules
Kadavath, H.; Jaremko, M.; Jaremko, L.; Biernat, J.; Mandelkow, E. & Zweckstetter, M. (2015)
Angewandte Chemie International Edition, 54(35) pp. 10347-10351. DOI: https://doi.org/10.1002/ange.201501714
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Details
- Authors
- Kadavath, Harindranath; Jaremko, Mariusz; Jaremko, Lukasz; Biernat, Jacek; Mandelkow, Eckhard; Zweckstetter, Markus
- 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 beta-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.
- Issue Date
- 2015
- Status
- published
- Publisher
- Wiley-v C H Verlag Gmbh
- Journal
- Angewandte Chemie International Edition
- ISSN
- 1521-3773; 1433-7851