The ability of the Ndc80 complex to bind two Dam1 complex rings is important for chromosome attachment, and the distance between the two rings is vital for supporting growth.

Quantitative experiments and theory show that the tension-dependent regulation of NDC80 binding to kinetochore microtubules arises from a combination of the changing Aurora B concentration at NDC80 and the nonlinearity of Aurora B autoactivation.

Multiple NDC80 complexes in the outer kinetochore cooperate to bind the ends of depolymerizing microtubules and harness their power stroke.

Binding of two macromolecular complexes allows kinetochores to capture force produced by the depolymerising ends of microtubules, allowing chromosomes to be transmitted from a mother cell to its two daughters.

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.

Flexibility of Ndc80 provides an inherent mode of regulation for the conserved kinetochore complex, unique from well-studied phospho-regulation.

Extensive cytological and biochemical analyses show that the conserved Sf3A2 and Prp31 splicing factors bind microtubules and the Ndc80 complex, playing direct mitotic functions in both Drosophila and human mitosis.

The centromeric protein CENP-T assembles the microtubule-binding interface of kinetochores through direct recruitment of two Ndc80 complexes and indirect recruitment of a third one through the Mis12 complex.

A key protein involved in the segregation of meiotic chromosomes is produced 'just in time' by the regulated expression of two mRNA isoforms.

Meiotic cells inhibit two distinct steps of replisome assembly with multiple kinases to prevent DNA replication between Meiosis I and Meiosis II.