Journal Article

DZNE-2020-04402

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Folding of the Tau Protein on Microtubules.

Kadavath, H. (First author)DZNE* ; Jaremko, M.DZNE* ; Jaremko, L.DZNE* ; Biernat, J.DZNE* ; Mandelkow, E.DZNE* ; Zweckstetter, M. (Last author)DZNE*

2015
Wiley-VCH Weinheim

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Please use a persistent id in citations: doi:10.1002/anie.201501714

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.

Keyword(s): Amyloid: chemistry (MeSH) ; Humans (MeSH) ; Magnetic Resonance Spectroscopy (MeSH) ; Microtubules: chemistry (MeSH) ; Protein Conformation (MeSH) ; Protein Folding (MeSH) ; tau Proteins: chemistry (MeSH) ; Amyloid ; tau Proteins

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Contributing Institute(s):

1. Structural Biology in Dementia (AG Zweckstetter)
2. Structural Principles of Neurodegeneration (AG Mandelkow 1 ; AG Mandelkow 1)

Research Program(s):

1. 342 - Disease Mechanisms and Model Systems (POF3-342) (POF3-342)

Appears in the scientific report 2015

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Database coverage:
; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; IF >= 10 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection

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