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

Yunior Cabrales Fontela1,2,3, Harindranath Kadavath1,3, Jacek Biernat4

  • 1Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Von-Siebold-Strasse 3a, 37075, Göttingen, Germany.

Nature Communications
|December 8, 2017
PubMed

Insights

Microtubule-associated proteins like Tau bind actin filaments through dynamic helical segments. This interaction, crucial for cytoskeletal cross-linking, is modulated by Tau

Area of Science:

  • Biochemistry
  • Cell Biology
  • Neuroscience

Background:

  • Microtubule-associated proteins (MAPs) regulate microtubule dynamics and actin filament interactions.
  • Aberrant Tau protein interaction with actin is implicated in Alzheimer's disease synaptic impairment.

Purpose of the Study:

  • To elucidate the molecular mechanism of Tau binding to actin filaments.
  • To understand how Tau-actin interactions contribute to cytoskeletal organization and disease pathology.

Main Methods:

  • Biochemical assays to study Tau-actin binding kinetics.
  • Structural modeling to visualize Tau-actin complex formation.
  • Site-directed mutagenesis and phosphorylation studies.

Main Results:

  • Tau binds actin filaments via multiple short helical segments in a dynamic, multivalent manner.
  • A single helix mediates Tau binding to actin, while at least two are required for actin bundling.
  • Phosphorylation of Tau at serine 262 reduces its binding affinity to actin filaments.

Conclusions:

  • Tau's interaction with actin is metamorphic and multivalent, essential for actin bundling and cytoskeleton cross-linking.
  • Understanding Tau-actin dynamics provides insight into synaptic function and Alzheimer's disease pathogenesis.

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