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Cdc25A abundance fluctuates periodically during the cell division cycle and is mainly regulated by the ubiquitin-proteasome system, through the action of two ubiquitin ligase complexes, which later promote complex/cyclosome and Skp1/Cul1/F-box proteins. Due to the presence of the destruction motif (KEN-box) in Cdc25A, ubiquitination and degradation occur at the mitotic outlet and G1, while phosphorylation events modulate the stability of Cdc25A protein in the S phase, both in undisturbed cells and in cells exposed to DNA damage agents or DNA replication inhibitors.
