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  Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.

Kadavath, H., Hofele, R. V., Biernat, J., Kumar, S., Tepper, K., Urlaub, H., et al. (2015). Tau stabilizes microtubules by binding at the interface between tubulin heterodimers. Proceedings of the National Academy of Sciences of the United States of America, 112(24), 7501-7506. doi:10.1073/pnas.1504081112.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-7D72-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CED0-D
Genre: Journal Article

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Kadavath, H.1, Author              
Hofele, R. V.2, Author              
Biernat, J., Author
Kumar, S., Author
Tepper, K., Author
Urlaub, H.2, Author              
Mandelkow, E., Author
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_578571              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: The structure, dynamic behavior, and spatial organization of microtubules are regulated by microtubule-associated proteins. An important microtubule-associated protein is the protein Tau, because its microtubule interaction is impaired in the course of Alzheimer’s disease and several other neurodegenerative diseases. Here, we show that Tau binds to microtubules by using small groups of evolutionary conserved residues. The binding sites are formed by residues that are essential for the pathological aggregation of Tau, suggesting competition between physiological interaction and pathogenic misfolding. Tau residues in between the microtubule-binding sites remain flexible when Tau is bound to microtubules in agreement with a highly dynamic nature of the Tau–microtubule interaction. By binding at the interface between tubulin heterodimers, Tau uses a conserved mechanism of microtubule polymerization and, thus, regulation of axonal stability and cell morphology.

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Language(s): eng - English
 Dates: 2015-06-01
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.1504081112
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 112 (24) Sequence Number: - Start / End Page: 7501 - 7506 Identifier: -