Self-repair protects microtubules from destruction by molecular motors

Nat Mater. 2021 Jun;20(6):883-891. doi: 10.1038/s41563-020-00905-0. Epub 2021 Jan 21.

Abstract

Microtubule instability stems from the low energy of tubulin dimer interactions, which sets the growing polymer close to its disassembly conditions. Molecular motors use ATP hydrolysis to produce mechanical work and move on microtubules. This raises the possibility that the mechanical work produced by walking motors can break dimer interactions and trigger microtubule disassembly. We tested this hypothesis by studying the interplay between microtubules and moving molecular motors in vitro. Our results show that molecular motors can remove tubulin dimers from the lattice and rapidly destroy microtubules. We also found that dimer removal by motors was compensated for by the insertion of free tubulin dimers into the microtubule lattice. This self-repair mechanism allows microtubules to survive the damage induced by molecular motors as they move along their tracks. Our study reveals the existence of coupling between the motion of molecular motors and the renewal of the microtubule lattice.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Microtubules / metabolism*
  • Models, Biological
  • Molecular Motor Proteins / metabolism*
  • Movement*

Substances

  • Molecular Motor Proteins