The growth speed of microtubules with XMAP215-coated beads coupled to their ends is increased by tensile force

Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):14670-5. doi: 10.1073/pnas.1218053110. Epub 2013 Aug 20.


The generation of pulling and pushing forces is one of the important functions of microtubules, which are dynamic and polarized structures. The ends of dynamic microtubules are able to form relatively stable links to cellular structures, so that when a microtubule grows it can exert a pushing force and when it shrinks it can exert a pulling force. Microtubule growth and shrinkage are tightly regulated by microtubule-associated proteins (MAPs) that bind to microtubule ends. Given their localization, MAPs may be exposed to compressive and tensile forces. The effect of such forces on MAP function, however, is poorly understood. Here we show that beads coated with the microtubule polymerizing protein XMAP215, the Xenopus homolog of Dis1 and chTOG, are able to link stably to the plus ends of microtubules, even when the ends are growing or shrinking; at growing ends, the beads increase the polymerization rate. Using optical tweezers, we found that tensile force further increased the microtubule polymerization rate. These results show that physical forces can regulate the activity of MAPs. Furthermore, our results show that XMAP215 can be used as a handle to sense and mechanically manipulate the dynamics of the microtubule tip.

Keywords: microtubule dynamics; microtubule polymerase; optical trap.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Kinetics
  • Microspheres*
  • Microtubule-Associated Proteins / metabolism*
  • Microtubules / chemistry
  • Microtubules / metabolism
  • Microtubules / physiology*
  • Polymerization
  • Protein Binding
  • Swine
  • Tensile Strength / physiology*
  • Tubulin / metabolism
  • Xenopus Proteins / metabolism*
  • Xenopus laevis


  • CKAP5 protein, Xenopus
  • Microtubule-Associated Proteins
  • Tubulin
  • Xenopus Proteins