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.

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.

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.

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.

Microtubule nucleation from the nuclear envelope in fission yeast involves repurposing of nuclear export proteins for a non-export-related function, docking cytoplasmic proteins at nuclear pore complexes.

Antagonism between binding to unpolymerized subunits and to the lattice leads to a ratcheting model for the processive action of a microtubule polymerase.

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