In vitro reconstitution of mRNA motility reveals the basis of directionally biased motion by groups of motors, their response to potential obstacles, and the consequences of reaching microtubule ends.

The motor domains of dynein are sufficient to crosslink microtubules and slide them antiparallel to each other.

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

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.

A sequential reaction pathway involving TPX2, augmin and γ-TuRC governs the assembly and architecture of branched microtubule networks.

Quantitative microscopy and theory show that the size of Xenopus laevis egg extract spindles is controlled by a spatially-regulated autocatalytic growth mechanism driven by microtubule-stimulated microtubule nucleation.

Biochemical and cell biological analyses reveal that the Astrin-SKAP complex acts to stabilize kinetochore-microtubule interactions through its intrinsic microtubule binding activity and its association with the Ndc80 complex, the core component of the kinetochore-microtubule interface.

A combination of cryo-electron microscopy of TPX2 bound to microtubules and in vitro reconstitution experiments reveals a novel microtubule interaction mode that explains how TPX2 promotes microtubule nucleation and stabilization.

Using linked TOG domains that each bind a curved conformation of αβ-tubulin, a microtubule polymerase catalyzes fast elongation by concentrating αβ-tubulin near the polymer end.

The budding yeast kinesin Kip2 is a polymerase that uses its processive motility in a positive feedback loop to promote microtubule growth.