A phospho-switch to trigger mitotic chromosome condensation

One of the most eye-catching events in cell biology is the condensation of chromosomes. During mitosis, the diffuse interphase chromatin rearranges into compact, rod-shaped chromosomes that can be precisely segregated between the daughter cells. This drastic reorganization of the DNA relies on condensin I and II complexes, large ring-shaped ATPases that extrude and stabilize loops of DNA. Since condensin II is always present in the nucleous its activity is repressed by the protein MCPH1 during interphase. But what are the molecular mechanisms regulating the activation of condensin II? New evidence suggests that this activation depends on the interaction between the condensin II subunit CAP-G2 with the centromeric protein M18BP1. Both the repressor and the activator bind on the same subunit of condensin II and their alternative binding is regulated by phosphorylation, which acts as the signal to trigger DNA condensation by condensin II.