Folding of the Tau Protein on Microtubules

Harindranath Kadavath, Mariusz Jaremko, Lukasz Jaremko, Jacek Biernat, Eckhard Mandelkow, Markus Zweckstetter*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

99 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)10347-10351
Number of pages5
JournalAngewandte Chemie - International Edition
Issue number35
StatePublished - Aug 1 2015


  • Alzheimer's disease
  • NMR spectroscopy
  • Tau protein
  • microtubules
  • structure elucidation

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)


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