Regulation of PP6 phosphatase activity by Plk1 in vitro.

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Regulation of PP6 phosphatase activity by Plk1 in vitro. Regulation of PP6 phosphatase activity by Plk1 in vitro. (A and B) Western blotting (A) and quantification (B) of Aurora A (AurA) phosphorylation at Thr288 in mitotically arrested HeLa cells treated with increasing amounts of Plk1 inhibitor, BI2536. Lamin A/C was a loading control. (C) Followed by Western blotting for total and phosphorylated (Thr288) Aurora A after preincubation with PP6R2-PP6c and CDK1–cyclin B, Plk1, or both in in vitro kinase/phosphatase assays, as indicated (top). (D) Western blot analysis of wild-type (WT) and Plk1 phosphorylation site mutants of PP6R2 holoenzymes containing PP6c, in vitro. (E) Representative Western blots of total and phosphorylated (Thr288) Aurora A (E) under basal conditions in vitro (−) or upon incubation with wild-type or mutant PP6R2 holoenzyme described in (D). Blots (A to E) are representative (n = 3) of and quantified data (B, C, and E) are means ± SD of three biological replicates. *P < 0.05 and **P < 0.01. Arminja N. Kettenbach et al., Sci. Signal. 2018;11:eaaq1441 ©2018 by American Association for the Advancement of Science