Local Nucleation of Microtubule Bundles through Tubulin Concentration into a Condensed Tau Phase

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • Amayra Hernández-Vega - , Max Planck Institute of Molecular Cell Biology and Genetics (Author)
  • Marcus Braun - , Chair of BioNano-Tools (Author)
  • Lara Scharrel - , Chair of BioNano-Tools, Max Planck Institute of Molecular Cell Biology and Genetics (Author)
  • Marcus Jahnel - , Chair of Biophysics, Max Planck Institute of Molecular Cell Biology and Genetics (Author)
  • Susanne Wegmann - , Harvard University (Author)
  • Bradley T. Hyman - , Harvard University (Author)
  • Simon Alberti - , Max Planck Institute of Molecular Cell Biology and Genetics (Author)
  • Stefan Diez - , Chair of BioNano-Tools, Max Planck Institute of Molecular Cell Biology and Genetics (Author)
  • Anthony A. Hyman - , Max Planck Institute of Molecular Cell Biology and Genetics (Author)

Abstract

Non-centrosomal microtubule bundles play important roles in cellular organization and function. Although many diverse proteins are known that can bundle microtubules, biochemical mechanisms by which cells could locally control the nucleation and formation of microtubule bundles are understudied. Here, we demonstrate that the concentration of tubulin into a condensed, liquid-like compartment composed of the unstructured neuronal protein tau is sufficient to nucleate microtubule bundles. We show that, under conditions of macro-molecular crowding, tau forms liquid-like drops. Tubulin partitions into these drops, efficiently increasing tubulin concentration and driving the nucleation of microtubules. These growing microtubules form bundles, which deform the drops while remaining enclosed by diffusible tau molecules exhibiting a liquid-like behavior. Our data suggest that condensed compartments of microtubule bundling proteins could promote the local formation of microtubule bundles in neurons by acting as non-centrosomal microtubule nucleation centers and that liquid-like tau encapsulation could provide both stability and plasticity to long axonal microtubule bundles.

Details

Original languageEnglish
Pages (from-to)2304-2312
Number of pages9
JournalCell reports
Volume20
Issue number10
Publication statusPublished - 5 Sep 2017
Peer-reviewedYes

External IDs

PubMed 28877466

Keywords

Research priority areas of TU Dresden

Keywords

  • cytoskeleton, drops, intrinsically disordered proteins, liquid-like, microtubule bundles, multivalency, nucleation, phase separation, tau, tubulin