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Cells are constantly threatened by multiple sources of genotoxic stress that cause  DNA  damage. To maintain genome integrity, cells have developed a coordinated signalling network called  DNA  damage response ( DDR ). While multiple kinases have been thoroughly studied during  DDR  activation, the role of protein dephosphorylation in the damage response remains elusive. Here, we show that the phosphatase Cdc14 is essential to fulfil recombinational  DNA  repair in budding yeast. After  DNA  double‐strand break ( DSB ) generation, Cdc14 is transiently released from the nucleolus and activated. In this state, Cdc14 targets the spindle pole body ( SPB ) component Spc110 to counterbalance its phosphorylation by cyclin‐dependent kinase (Cdk). Alterations in the Cdk/Cdc14‐dependent phosphorylation status of Spc110, or its inactivation during the induction of a  DNA  lesion, generate abnormal oscillatory  SPB  movements that disrupt  DSB ‐ SPB  interactions. Remarkably, these defects impair  DNA  repair by homologous recombination indicating that  SPB  integrity is essential during the repair process. Together, these results show that Cdc14 promotes spindle stability and  DSB ‐ SPB  tethering during  DNA  repair, and imply that metaphase spindle maintenance is a critical feature of the repair process.

Stabilization of the metaphase spindle by Cdc14 is required for recombinational DNA repair