Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro

PLoS One. 2012;7(8):e42218. doi: 10.1371/journal.pone.0042218. Epub 2012 Aug 1.

Abstract

Kinesin-1 plays a major role in anterograde transport of intracellular cargo along microtubules. Currently, there is an ongoing debate of whether α-tubulin K40 acetylation directly enhances the velocity of kinesin-1 and its affinity to the microtubule track. We compared motor motility on microtubules reconstituted from acetylated and deacetylated tubulin. For both, single- and multi-motor in vitro motility assays, we demonstrate that tubulin acetylation alone does not affect kinesin-1 velocity and run length.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Animals
  • Kinesin / chemistry*
  • Kinesin / metabolism
  • Mice
  • Microtubules / chemistry*
  • Microtubules / metabolism
  • Tubulin / chemistry*
  • Tubulin / metabolism

Substances

  • Tubulin
  • Kinesin

Grant support

This work has been supported by funding from the Volkswagen Foundation (grant I/84 087–090), the Deutsche Forschungsgemeinschaft (DFG Heisenberg Program), the Max-Planck-Society, the Technische Universität Dresden and the European Research Council (ERC starting grant 242933). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.