J. Al-Bassam

This study investigates how the structural features of kinesin-5, specifically tail-motor domain interactions and minifilament length, influence microtubule sliding motility and spindle organization.

This study reveals that directionality switching of kinesin-5 Cin8 motors is caused by an asymmetric response to drag forces, identified through cluster-motility analysis and biophysical modeling.

This study shows the kinesin-5 tail domain regulates motor activity by modulating ATP hydrolysis and microtubule sliding, leading to slow motility and force generation.

The paper elucidates the structural mechanism by which TOG domain arrays in Alp14 recruit and polymerize tubulins through square-shaped assemblies that unfurl to facilitate polymerization.

This study reveals the structural basis for katanin self-assembly, showing how ATP binding and conformational changes regulate its oligomerization and microtubule-severing activity.