Cell division cycle 25C phosphatase (CDC25C) (CDC25C)

The Cell division cycle 25C phosphatase (CDC25C) is a dual-specificity phosphatase that acts as a key regulator of the cell cycle, primarily driving the G2/M transition by dephosphorylating inhibitory residues (Thr14 and Tyr15) on CDK1 in the cyclin B1/CDK1 complex, thereby activating mitosis entry. It features an N-terminal regulatory domain with phosphorylation and localization signals, including nuclear export/import sequences that shuttle it between cytoplasm and nucleus, and a conserved C-terminal catalytic domain with the HCX5R motif typical of tyrosine phosphatases. CDC25C activity forms a positive feedback loop with cyclin B1/CDK1, ensuring rapid, irreversible mitotic commitment, while DNA damage checkpoints involving CHK1/CHK2, ATM/ATR, and p53 phosphorylate and sequester it via 14-3-3 binding to prevent premature mitosis and allow repair. Overexpression or dysregulation of CDC25C promotes genomic instability and is frequently observed in cancers, positioning it as an attractive anticancer target due to its role in unchecked proliferation. Although no approved drugs directly target it, its inhibition could synergize with DNA-damaging chemotherapies by trapping cells in G2 phase.

Other names

Cdc25CM-phase inducer phosphatase 3