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

Slow conformational changes after drug binding rationalize selectivity, affinity and long on-target residence time for kinase inhibitors.

Phosphorylation of Aurora A does not trigger a population shift to the active state as previously thought, but instead switches the kinase on by tuning the structure and dynamics of a dynamically sampled subpopulation.

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.

Protein kinase A-driven increases in c-MYC protein expression and tumor cell proliferation can be blocked by eIF4A inhibitors, suggesting a potential new treatment option for patients with oncogenic PKA activation.

AurkA is imported into mitochondria at interphase, and it induces organelle elongation and enhances ATP production when over-expressed.

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

A histone modification that alters the nucleosome structure occurs in mitosis and promotes chromosome packaging and the timely removal of condensin I and cohesion, to achieve chromosome segregation.

Post-transcriptional regulation of Aurora Kinase A (AURKA) through alternative polyadenylation of its mRNA determines miRNA influence and is a feature of cell cycle-specific AURKA expression whose impairment leads to acquisition of cancer phenotypes.