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Updated: Aug 6, 2026

Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence (TIRF) Microscopy
Published on: July 20, 2022
Simulations of an Extended Tau/Tubulins Interface Reveal a Complex Disorder-Disorder Interplay Mediated by the
Jules Marien1, Chantal Prévost1, Sophie Sacquin-Mora1
1Laboratoire de Biochimie Théorique, Université Paris Cité, CNRS, 13 rue Pierre et Marie Curie, Paris75005, France.
Abstract:
Building on a complex between a tubulin protofilament (PF) and a fragment of the Tau protein containing residues 169 to 367, we investigate the dynamics of the disordered elements of the system, namely the tubulin C-terminal tails (CTTs) and the Tau protein, using classical all-atom molecular dynamics simulations. Our results show that CTTs adopt a hook-like dynamic pattern on the bare PF while remaining highly mobile. The binding of Tau on the PF surface alters the dynamics of the αI-CTTs in a sequence-dependent manner. While the repeat domains of Tau are mostly maintained on the PF by weak and strong binding patches with the tubulin cores, the Proline-Rich Region (PRR) relies on the wrapping phenomenon of αI-CTTs to fuzzily stabilize its interaction with the PF. Our study thus provides a deep dive into the dynamic interplay between the Tau protein and the CTTs of microtubules, the latter being characterized extensively using a variety of disorder-adapted metrics.
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