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  Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau

Fontela, Y. C., Kadavath, H., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017). Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau. Nature Communications, 8(1): 1981. doi:10.1038/s41467-017-02230-8.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0001-7900-7 Version Permalink: https://hdl.handle.net/21.11116/0000-0007-50E5-C
Genre: Journal Article

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https://www.nature.com/articles/s41467-017-02230-8 (Publisher version)
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Fontela, Yunior Cabrales1, Author
Kadavath, Harindranath1, Author
Biernat, Jacek1, Author
Riedel, Dietmar1, Author
Mandelkow, Eckhard1, 2, Author
Zweckstetter, Markus1, Author
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1external, ou_persistent22              
2Neuronal Cytoskeleton and Alzheimer's Disease, Cooperations, Center of Advanced European Studies and Research (caesar), Max Planck Society, Ludwig-Erhard-Allee 2, 53175 Bonn, DE, ou_2173677              

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 Abstract: Microtubule-associated proteins regulate microtubule dynamics, bundle actin filaments, and cross-link actin filaments with microtubules. In addition, aberrant interaction of the microtubule-associated protein Tau with filamentous actin is connected to synaptic impairment in Alzheimer's disease. Here we provide insight into the nature of interaction between Tau and actin filaments. We show that Tau uses several short helical segments to bind in a dynamic, multivalent process to the hydrophobic pocket between subdomains 1 and 3 of actin. Although a single Tau helix is sufficient to bind to filamentous actin, at least two, flexibly linked helices are required for actin bundling. In agreement with a structural model of Tau repeat sequences in complex with actin filaments, phosphorylation at serine 262 attenuates binding of Tau to filamentous actin. Taken together the data demonstrate that bundling of filamentous actin and cross-linking of the cellular cytoskeleton depend on the metamorphic and multivalent nature of microtubule-associated proteins.

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 Dates: 2017-12-072017-12-07
 Publication Status: Issued
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 Identifiers: ISI: 000417336600011
DOI: 10.1038/s41467-017-02230-8
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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 8 (1) Sequence Number: 1981 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723