The tubulin GTPase cycle structurally modulates the microtubule cap, causing lattice expansion, which is an intermediate state involved in phosphate release and regulatory signaling.

Biochemical, single molecule, cell and structural biology studies reveal an interaction between the kinesin-5 tail and motor domains regulating high-force production, which is critical for microtubule sliding motility.

Human chromosome-microtubule attachments are stabilised by Astrin-mediated dynamic delivery of PP1 phosphatase to the attachment site, which ensures the normal segregation of chromosomes.

The somatic Golgi acts as an asymmetric MTOC within Drosophila neurons, and this, together with the action Kinesin-2, helps maintain minus-end-out microtubule polarity with proximal dendrites.

In Caenorhabditis elegans, dendrites establish their unique microtubule polarity by localizing an organizing center behind the growing tip.

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

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.

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.

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