VRK1 kinase activation in response to DNA damage.
A, effect of serum withdrawal on the activity of VRK1. Endogenous VRK1 was immunoprecipitated from MCF7 cells either growing in 10% FBS (lane 1), serum-starved for 48 h (lane 2), or serum-starved for 48 h followed by 15 h in 10% FBS (lane 3). VRK1 activity was assayed in vitro for autophosphorylation and phosphorylation of GST-p53(1–85) fragment. B, kinase activity of endogenous VRK1 in response to DSBs. MCF7 cells were serum-starved and then treated with 2 Gy of ionizing radiation, 1 μm doxorubicin, or 50 μm etoposide. Endogenous VRK1 protein was immunoprecipitated and used in an in vitro kinase assay detecting its autophosphorylation and phosphorylation of GST-p53(1–85). C, detection of cell cycle markers by Western blot. MCF7 cells were grown in the presence of serum, serum-starved for 48 h, or serum-starved for 48 h followed by 15 h in serum. Extracts were blotted for phospho-Rb, cyclin D1, p27, VRK1, and actin. IP, immunoprecipitation; IB, immunoblot.