Effects of α-tubulin K40 acetylation and detyrosination on kinesin-1 motility in a purified system.

ABSTRACT: Long-range transport in cells is achieved primarily through motor-based transport along a network of microtubule tracks. Targeted transport by kinesin motors can be correlated with posttranslational modifications (PTMs) of the tubulin subunits in specific microtubules. To directly examine the influence of specific PTMs on kinesin-1 motility, we generated tubulin subunits that were either enriched in or lacking acetylation of α-tubulin lysine 40 (K40) or detyrosination of the α-tubulin C-terminal tail. We show that K40 acetylation does not result in significant changes in kinesin-1's landing rate or motility parameters (velocity and run length) across experimental conditions. In contrast, detyrosination causes a moderate increase in kinesin-1's landing rate. The fact that the effects of det

SUBMITTER: Kaul N 

PROVIDER: S-EPMC4070028 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature