Journal
PLOS ONE
Volume 7, Issue 8, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0042218
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Funding
- Volkswagen Foundation [I/84 087-090]
- Deutsche Forschungsgemeinschaft (DFG Heisenberg Program)
- Max-Planck-Society
- Technische Universitat Dresden
- European Research Council (ERC) [242933]
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Kinesin-1 plays a major role in anterograde transport of intracellular cargo along microtubules. Currently, there is an ongoing debate of whether alpha-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.
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