Tubulin Acetylation Alone Does Not Affect Kinesin-1 Velocity and Run Length In Vitro
Open Access
- 1 August 2012
- journal article
- research article
- Published by Public Library of Science (PLoS) in PLOS ONE
- Vol. 7 (8), e42218
- https://doi.org/10.1371/journal.pone.0042218
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.This publication has 28 references indexed in Scilit:
- The Nucleotide-binding State of Microtubules Modulates Kinesin Processivity and the Ability of Tau to Inhibit Kinesin-mediated TransportJournal of Biological Chemistry, 2011
- Tracking Single Particles and Elongated Filaments with Nanometer PrecisionBiophysical Journal, 2011
- Huntingtin Controls Neurotrophic Support and Survival of Neurons by Enhancing BDNF Vesicular Transport along MicrotubulesCell, 2004
- The Spatial and Temporal Dynamics of Pleckstrin Homology Domain Binding at the Plasma Membrane Measured by Imaging Single Molecules in Live Mouse MyoblastsOnline Journal of Public Health Informatics, 2004
- Microtubules provide directional cues for polarized axonal transport through interaction with kinesin motor headThe Journal of cell biology, 2003
- Huntington's DiseaseNeuroMolecular Medicine, 2003
- HDAC6 is a microtubule-associated deacetylaseNature, 2002
- KIF1D is a fast non-processive kinesin that demonstrates novel K-loop-dependent mechanochemistryThe EMBO Journal, 2001
- Engineering the Processive Run Length of the Kinesin MotorThe Journal of cell biology, 2000
- Temperature Dependence of Force, Velocity, and Processivity of Single Kinesin MoleculesBiochemical and Biophysical Research Communications, 2000