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@ARTICLE{CabralesFontela:139653,
      author       = {Cabrales Fontela, Yunior and Kadavath, Harindranath and
                      Biernat, Jacek and Riedel, Dietmar and Mandelkow, Eckhard
                      and Zweckstetter, Markus},
      title        = {{M}ultivalent cross-linking of actin filaments and
                      microtubules through the microtubule-associated protein
                      {T}au.},
      journal      = {Nature Communications},
      volume       = {8},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DZNE-2020-05975},
      pages        = {1981},
      year         = {2017},
      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.},
      keywords     = {Actin Cytoskeleton: chemistry / Actin Cytoskeleton:
                      metabolism / Actin Depolymerizing Factors: chemistry / Actin
                      Depolymerizing Factors: metabolism / Alzheimer Disease:
                      pathology / Humans / Hydrophobic and Hydrophilic
                      Interactions / Microtubule-Associated Proteins /
                      Microtubules: metabolism / Molecular Docking Simulation /
                      Phosphorylation / Protein Interaction Domains and Motifs /
                      Serine: metabolism / tau Proteins: chemistry / tau Proteins:
                      metabolism / Actin Depolymerizing Factors (NLM Chemicals) /
                      Microtubule-Associated Proteins (NLM Chemicals) / tau
                      Proteins (NLM Chemicals) / Serine (NLM Chemicals)},
      cin          = {AG Zweckstetter / AG Mandelkow 1},
      ddc          = {500},
      cid          = {I:(DE-2719)1410001 / I:(DE-2719)1013014},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29215007},
      pmc          = {pmc:PMC5719408},
      doi          = {10.1038/s41467-017-02230-8},
      url          = {https://pub.dzne.de/record/139653},
}