Native kinesin-1 does not bind preferentially to GTP-tubulin-rich microtubules in vitro.

ABSTRACT: Molecular motors such as kinesin-1 work in small teams to actively shuttle cargos in cells, for example in polarized transport in axons. Here, we examined the potential regulatory role of the nucleotide state of tubulin on the run length of cargos carried by multiple kinesin motors, using an optical trapping-based in vitro assay. Based on a previous report that kinesin binds preferentially to GTP-tubulin-rich microtubules, we anticipated that multiple-kinesin cargos would run substantially greater distances along GMPCPP microtubules than along GDP microtubules. Surprisingly, we did not uncover any significant differences in run length between microtubule types. A combination of single-molecule experiments, comparison with previous theory, and classic microtubule affinity pulldown assays re

SUBMITTER: Li Q 

PROVIDER: S-EPMC5752144 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature