Fig. 6

SRSF10 activates CDC25A through Ser178 dephosphorylation. A CDC25A associated cell cycle pathway and Ser178 phosphorylating status in response to SRSF10. Rabusertib is a highly selective CHK1 inhibitor that could restrain CDC25A phosphorylation. B Ser178 phosphorylation did not affect CDC25A stability. Ser178 substitution to alanine (A) suspended phosphorylation while glutamic acid (E) mutation could mimic constant phosphorylation. The protein stability assay was performed using CHX + MG132 intervention. C Ser178 phosphorylation affected CDC25A subcellular localization. Dephosphorylated CDC25A (S178A) was inclined to nuclear retention, whereas constant phosphorylated CDC25A (S178E) showed extranuclear abundance. Scale bars, 20 μm. D, E, F, G The dephosphorylation of CDC25A in Ser178 contributed to the cell viability (D), proliferation (E), cell cycle (F), and invasion (G) ability of HCC. Data are presented as the mean ± SD value of three biological replicates. **p < 0.01, ***p < 0.001 vs. WT, t test. See representative images in Supplementary Fig. 10