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A simple mechanism relying on microtubule rescues occurring at midzone edges allows fission yeast spindles to elongate during anaphase B while maintaining microtubule overlaps, without the need to precisely regulate microtubule growth speed.

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.

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.

Structural rearrangements of meiotic spindles during the transition from metaphase to anaphase can be controlled by local changes of microtubule dynamics, such as nucleation and/or turnover, and that katanin promotes microtubule turnover by severing microtubules near the chromosomes.

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, 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.

Autocatalytic growth of a microtubule polymer network allows extremely large egg cells to self-organize and divide rapidly.

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

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.

Specific glutamylation of some α-tubulin isotypes affects kinesin-1 localization and transport processes that depend on it, but their absence can speed up transport, possibly explaining why some large cells express α-tubulin isotypes that are not glutamylated.