The cell cycle progression is governed by a family of kinases (cdk: cyclin dependent kinases) whose activities are regulated by binding to regulatory subunits called cyclins. During the cell cycle and activate form specific pairs of cdk and cyclins. The pair CDK1 with cyclins A and B governs the transition G 2 / M. During the cell cycle cdk levels remain relatively constant and the cyclins fluctuate, thus activating specific cdk.

Cyclin A accumulates at the beginning of S phase, contributing to the stimulation of DNA synthesis. Then the level of cyclin A remains high during G2 and is degraded in prometaphase. Cyclin B levels increase during G2 and is then binds to CDK1. This complex leads to the metaphase cycle where cyclin B is degraded, although much later than cyclin A. Signals that dictate cyclin degradation in prometaphase are still controversial. In this study of Matthew et al., Department of Cell Biology, University of Barcelona, we show that cyclin A can be acetylated in vivo and in vitro by an acetyltransferase P / CAF in four lysines located at the N-terminal .

In mitosis maximum acetylation occurs simultaneously to ubiquitination, which marks the importance of acetylation on the stability of cyclin A In addition, cells were treated with inhibitors of histone deacetylases, acetylation of cyclin A increases and stability decreases, which confirms the role of acetylation in the degradation of cyclin A. In summary, the specific acetylation of certain lysines of cyclin A is crucial for the stability of the same and has a role regulating the activity of cdk-cyclin pair A.