Details

Autor(en) / Beteiligte

• Kadavath, Harindranath
• Jaremko, Mariusz
• Jaremko, Łukasz
• Biernat, Jacek
• Mandelkow, Eckhard
• Zweckstetter, Markus

Titel

Folding of the Tau Protein on Microtubules

Ist Teil von

• Angewandte Chemie (International ed.), 2015-08, Vol.54 (35), p.10347-10351

Auflage

International ed. in English

Ort / Verlag

Weinheim: WILEY-VCH Verlag

Erscheinungsjahr

2015

Quelle

MEDLINE

Beschreibungen/Notizen

• 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. Tau the line: NMR spectroscopy shows that the 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 forms a β‐sheet structure in amyloid fibrils, the conserved hexapeptides at the beginning of the second and third repeats in Tau adopt a hairpin conformation when bound to microtubules. Thus, binding to microtubules stabilizes a unique conformation in Tau.