Motor usage imprints microtubule stability along the shaft

Dev Cell. 2022 Jan 10;57(1):5-18.e8. doi: 10.1016/j.devcel.2021.11.019. Epub 2021 Dec 8.

Abstract

Tubulin dimers assemble into dynamic microtubules, which are used by molecular motors as tracks for intracellular transport. Organization and dynamics of the microtubule network are commonly thought to be regulated at the polymer ends, where tubulin dimers can be added or removed. Here, we show that molecular motors running on microtubules cause exchange of dimers along the shaft in vitro and in cells. These sites of dimer exchange act as rescue sites where depolymerizing microtubules stop shrinking and start re-growing. Consequently, the average length of microtubules increases depending on how frequently they are used as motor tracks. An increase of motor activity densifies the cellular microtubule network and enhances cell polarity. Running motors leave marks in the shaft, serving as traces of microtubule usage to organize the polarity landscape of the cell.

Keywords: cell polarity; cell symmetry; dynamics; in vitro; kinesin; microtubule; microtubule damage; microtubule lifetime; microtubule network; network density; repair; rescue; tubulin exchange.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Depolymerizing Factors / metabolism
  • Actin Depolymerizing Factors / physiology
  • Cell Polarity / physiology
  • HeLa Cells
  • Humans
  • Kinesins / metabolism
  • Kinesins / physiology*
  • Microtubules / physiology*
  • Molecular Motor Proteins / metabolism
  • Molecular Motor Proteins / physiology
  • Tubulin / physiology

Substances

  • Actin Depolymerizing Factors
  • KIF5B protein, human
  • Molecular Motor Proteins
  • Tubulin
  • Kinesins