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000139653 1001_ $$0P:(DE-2719)2812335$$aCabrales Fontela, Yunior$$b0$$eFirst author$$udzne
000139653 245__ $$aMultivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau.
000139653 260__ $$a[London]$$bNature Publishing Group UK$$c2017
000139653 264_1 $$2Crossref$$3online$$bSpringer Science and Business Media LLC$$c2017-12-07
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000139653 520__ $$aMicrotubule-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.
000139653 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
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000139653 650_7 $$2NLM Chemicals$$aActin Depolymerizing Factors
000139653 650_7 $$2NLM Chemicals$$aMicrotubule-Associated Proteins
000139653 650_7 $$2NLM Chemicals$$atau Proteins
000139653 650_7 $$0452VLY9402$$2NLM Chemicals$$aSerine
000139653 650_2 $$2MeSH$$aActin Cytoskeleton: chemistry
000139653 650_2 $$2MeSH$$aActin Cytoskeleton: metabolism
000139653 650_2 $$2MeSH$$aActin Depolymerizing Factors: chemistry
000139653 650_2 $$2MeSH$$aActin Depolymerizing Factors: metabolism
000139653 650_2 $$2MeSH$$aAlzheimer Disease: pathology
000139653 650_2 $$2MeSH$$aHumans
000139653 650_2 $$2MeSH$$aHydrophobic and Hydrophilic Interactions
000139653 650_2 $$2MeSH$$aMicrotubule-Associated Proteins
000139653 650_2 $$2MeSH$$aMicrotubules: metabolism
000139653 650_2 $$2MeSH$$aMolecular Docking Simulation
000139653 650_2 $$2MeSH$$aPhosphorylation
000139653 650_2 $$2MeSH$$aProtein Interaction Domains and Motifs
000139653 650_2 $$2MeSH$$aSerine: metabolism
000139653 650_2 $$2MeSH$$atau Proteins: chemistry
000139653 650_2 $$2MeSH$$atau Proteins: metabolism
000139653 7001_ $$0P:(DE-2719)2811307$$aKadavath, Harindranath$$b1$$udzne
000139653 7001_ $$0P:(DE-2719)2810342$$aBiernat, Jacek$$b2$$udzne
000139653 7001_ $$aRiedel, Dietmar$$b3
000139653 7001_ $$0P:(DE-2719)2541671$$aMandelkow, Eckhard$$b4$$udzne
000139653 7001_ $$0P:(DE-2719)2810591$$aZweckstetter, Markus$$b5$$eLast author$$udzne
000139653 77318 $$2Crossref$$3journal-article$$a10.1038/s41467-017-02230-8$$b : Springer Science and Business Media LLC, 2017-12-01$$n1$$p1981$$tNature Communications$$v8$$x2041-1723$$y2017
000139653 773__ $$0PERI:(DE-600)2553671-0$$a10.1038/s41467-017-02230-8$$gVol. 8, no. 1, p. 1981$$n1$$p1981$$q8:1<1981$$tNature Communications$$v8$$x2041-1723$$y2017
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000139653 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC5719408
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