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001     139653
005     20240511120150.0
024 7 _ |a 10.1038/s41467-017-02230-8
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037 _ _ |a DZNE-2020-05975
041 _ _ |a English
082 _ _ |a 500
100 1 _ |a Cabrales Fontela, Yunior
|0 P:(DE-2719)2812335
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245 _ _ |a Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau.
260 _ _ |a [London]
|c 2017
|b Nature Publishing Group UK
264 _ 1 |3 online
|2 Crossref
|b Springer Science and Business Media LLC
|c 2017-12-07
264 _ 1 |3 print
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|b Springer Science and Business Media LLC
|c 2017-12-01
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520 _ _ |a 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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650 _ 7 |a Actin Depolymerizing Factors
|2 NLM Chemicals
650 _ 7 |a Microtubule-Associated Proteins
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650 _ 7 |a tau Proteins
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650 _ 7 |a Serine
|0 452VLY9402
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650 _ 2 |a Actin Cytoskeleton: chemistry
|2 MeSH
650 _ 2 |a Actin Cytoskeleton: metabolism
|2 MeSH
650 _ 2 |a Actin Depolymerizing Factors: chemistry
|2 MeSH
650 _ 2 |a Actin Depolymerizing Factors: metabolism
|2 MeSH
650 _ 2 |a Alzheimer Disease: pathology
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Hydrophobic and Hydrophilic Interactions
|2 MeSH
650 _ 2 |a Microtubule-Associated Proteins
|2 MeSH
650 _ 2 |a Microtubules: metabolism
|2 MeSH
650 _ 2 |a Molecular Docking Simulation
|2 MeSH
650 _ 2 |a Phosphorylation
|2 MeSH
650 _ 2 |a Protein Interaction Domains and Motifs
|2 MeSH
650 _ 2 |a Serine: metabolism
|2 MeSH
650 _ 2 |a tau Proteins: chemistry
|2 MeSH
650 _ 2 |a tau Proteins: metabolism
|2 MeSH
700 1 _ |a Kadavath, Harindranath
|0 P:(DE-2719)2811307
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|u dzne
700 1 _ |a Biernat, Jacek
|0 P:(DE-2719)2810342
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700 1 _ |a Riedel, Dietmar
|b 3
700 1 _ |a Mandelkow, Eckhard
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700 1 _ |a Zweckstetter, Markus
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773 1 8 |a 10.1038/s41467-017-02230-8
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773 _ _ |a 10.1038/s41467-017-02230-8
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