title: Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro.
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.
authors.affiliation: B CUBE-Center for Molecular Bioengineering, Technische Universität Dresden, Dresden, Germany.
authors.forename: Wilhelm J
authors.initials: WJ
authors.lastname: Walter
authors.forename: Václav
authors.initials: V
authors.lastname: Beránek
authors.forename: Elisabeth
authors.initials: E
authors.lastname: Fischermeier
authors.forename: Stefan
authors.initials: S
authors.lastname: Diez
mesh_terms: D000107:Acetylation; D000818:Animals; D016547:Kinesins / Q000737:chemistry* / Q000378:metabolism; D051379:Mice; D008870:Microtubules / Q000737:chemistry* / Q000378:metabolism; D014404:Tubulin / Q000737:chemistry* / Q000378:metabolism
chemical_list: D014404:Tubulin; D016547:Kinesins