Related Experiment Video
Updated: Jun 4, 2026

Motility of Single Molecules and Clusters of Bi-Directional Kinesin-5 Cin8 Purified from S. cerevisiae Cells
Published on: February 2, 2022
Two-state displacement by the kinesin-14 Ncd stalk
Mark A Hallen1, Zhang-Yi Liang, Sharyn A Endow
1Department of Cell Biology, Structural Biology & Biophysics Program, Duke University Medical Center, Durham, NC 27710, USA. mark.hallen@duke.edu
Abstract:
The nonprocessive kinesin-14 Ncd motor binds to microtubules and hydrolyzes ATP, undergoing a single displacement before releasing the microtubule. A lever-like rotation of the coiled-coil stalk is thought to drive Ncd displacements or steps along microtubules. Crystal structures and cryoelectron microscopy reconstructions imply that stalk rotation is correlated with ADP release and microtubule binding by the motor. Here we report FRET assays showing that the end of the stalk is more than ~9nm from the microtubule when wild-type Ncd binds microtubules without added nucleotide, but the stalk is within ~6nm of the microtubule surface when the microtubule-bound motor binds an ATP analogue, matching the rotated state observed in crystal structures. We propose that the stalk rotation is initiated when the motor binds to microtubules and releases ADP, and is completed when ATP binds.
Related Concept Videos
The Movement of Organelles and Vesicles
Destabilization of Microtubules
Forces Acting on Chromosomes
Microtubules and motor proteins exert two types of forces on...
Anaphase A and B
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...
Mechanism of Ciliary Motion
The cilia are made up of microtubules in a 9+2 arrangement, with nine microtubule doublet ring bundles, surrounding a pair of central singlet microtubule bundles. The doublet microtubule bundles are...
Attachment of Sister Chromatids

