Cryo-electron microscopy reconstructions of two microtubule-bound transport kinesins at 7 Å resolution reveal how microtubule track binding stimulates ADP release, primes the active site for ATP binding and enables force generation.

Microtubule attachment fundamentally modifies kinesin's behavior by triggering a ‘clamshell’ opening of the nucleotide cleft, subsequently reversed by ATP binding, that couples to cargo translocation.

After developing a force-gliding assay with nanometer and piconewton precision, it is concluded that multiple kinesins driving a single cargo induces tension, resulting in smooth cargo transport, even with roadblocks.

Dynein bypasses obstacles on microtubules more efficiently than single kinesin, and kinesins overcome this limitation when transporting intracellular cargos in teams.

The function and distribution of kinesin motors on exocytotic vesicles is dissected and visualized through a combination of gene knockout experiments, high-resolution microscopy and advanced data analysis.

Cryo-electron microscopy reveals how kinesin-binding protein inhibits microtubule attachment in a subset of kinesins.

The structural and functional analysis demonstrates the mechanism of dual functional, motility and microtubule depolymerization in a unique motor, KIF19A.

A novel algorithm is used to solve the first 3D reconstruction of a stepping kinesin dimer on microtubules, directly visualizing the conformational effects of inter-head strain and giving novel insights into the motility mechanism.

Kinesin-like calmodulin-binding protein integrates microtubules and F-actin to assemble the cytoskeletal configuration needed for trichome formation.

Posterior determination of Drosophila oocyte is defined by competition between kinesin-1 removing posterior determinants from the cortex and myosin-V anchoring them.