BRSK2 expressed in insect cells specifically phosphorylates WEE1A, CDC25C, and CDC25B in an in vitro assay, but a kinase-dead mutant does not. Overexpression of BRSK2 in HeLa cells results in increased phosphorylation of CDC25C. DNA damage induced by ultraviolet (UV) irradiation or methyl methane sulfonate, but not by ionizing radiation, enhances endogenous BRSK2 kinase activity in a caffeine-sensitive manner and causes translocation of BRSK2 from the cytoplasm to the nucleus. Overexpression of BRSK2 induces G2/M arrest in HeLa cells. Small interfering RNA against BRSK2 partly abrogates UV-induced G2/M arrest. BRSK2 may act as a checkpoint kinase upon DNA damage induced by UV irradiation or methyl methane sulfonate.

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