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Folding of the Tau Protein on Microtubules
Author(s) -
Kadavath Harindranath,
Jaremko Mariusz,
Jaremko Łukasz,
Biernat Jacek,
Mandelkow Eckhard,
Zweckstetter Markus
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201501714
Subject(s) - microtubule , biophysics , microtubule associated protein , folding (dsp implementation) , tau protein , chemistry , tubulin , protein folding , fibril , microbiology and biotechnology , crystallography , biology , biochemistry , medicine , electrical engineering , disease , pathology , alzheimer's disease , engineering
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.