Unknown

Dataset Information

0

Kar3Vik1, a member of the kinesin-14 superfamily, shows a novel kinesin microtubule binding pattern.


ABSTRACT: Kinesin-14 motors generate microtubule minus-end-directed force used in mitosis and meiosis. These motors are dimeric and operate with a nonprocessive powerstroke mechanism, but the role of the second head in motility has been unclear. In Saccharomyces cerevisiae, the Kinesin-14 Kar3 forms a heterodimer with either Vik1 or Cik1. Vik1 contains a motor homology domain that retains microtubule binding properties but lacks a nucleotide binding site. In this case, both heads are implicated in motility. Here, we show through structural determination of a C-terminal heterodimeric Kar3Vik1, electron microscopy, equilibrium binding, and motility that at the start of the cycle, Kar3Vik1 binds to or occludes two ??-tubulin subunits on adjacent protofilaments. The cycle begins as Vik1 collides with the microtubule followed by Kar3 microtubule association and ADP release, thereby destabilizing the Vik1-microtubule interaction and positioning the motor for the start of the powerstroke. The results indicate that head-head communication is mediated through the adjoining coiled coil.

SUBMITTER: Rank KC 

PROVIDER: S-EPMC3384419 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Kar3Vik1, a member of the kinesin-14 superfamily, shows a novel kinesin microtubule binding pattern.

Rank Katherine C KC   Chen Chun Ju CJ   Cope Julia J   Porche Ken K   Hoenger Andreas A   Gilbert Susan P SP   Rayment Ivan I  

The Journal of cell biology 20120601 7


Kinesin-14 motors generate microtubule minus-end-directed force used in mitosis and meiosis. These motors are dimeric and operate with a nonprocessive powerstroke mechanism, but the role of the second head in motility has been unclear. In Saccharomyces cerevisiae, the Kinesin-14 Kar3 forms a heterodimer with either Vik1 or Cik1. Vik1 contains a motor homology domain that retains microtubule binding properties but lacks a nucleotide binding site. In this case, both heads are implicated in motilit  ...[more]

Similar Datasets

| S-EPMC7063570 | biostudies-literature
| S-EPMC5700410 | biostudies-literature
| S-EPMC8604404 | biostudies-literature
| S-EPMC4720966 | biostudies-literature
| S-EPMC4220466 | biostudies-literature
| S-EPMC5668670 | biostudies-literature
| S-EPMC5461021 | biostudies-literature
| S-EPMC4395489 | biostudies-literature
| S-EPMC4548964 | biostudies-literature