An entropy switch controls the Aurora B autoactivation process through two distinct kinetic steps of phosphorylation.

Self-activating Aurora B kinase, opposed by an inhibitory phosphatase, forms spatial phosphorylation patterns during cell division.

Quantitative live-cell microscopy and molecular perturbations in Drosophila and human cells reveal a crosstalk between molecular 'rulers' (Aurora B) and 'clocks' (Cdk1) that coordinates mitotic exit in space and time.

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.

Direct live-cell imaging of human cells, combined with RNA-seq, qPCR and in vitro reconstitution essays, reveal that mitotic progression, arrest, exit or death is independent of de novo transcription.

The conserved chTOG protein is required to destabilize incorrect kinetochore-microtubule attachments.

The regulation of the core transcription factor Oct4 by the Aurkb-PP1 axis links the cell cycle to pluripotency programs in embryonic stem cells.

Shugoshin proteins help to align chromosomes so that copies of the same chromosome attach to microtubules from opposite poles during cell division.

The kinetoplastid parasite Trypanosoma brucei employs a unique mechanism to target the conserved Aurora B kinase to kinetochores and the central spindle.

Aurora A kinase, an anti-cancer drug target, can be activated by two independent mechanisms.