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. 2016 Jun 3;36(3):e00343. doi: 10.1042/BSR20160123

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© 2016 The Author(s)

This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution Licence 4.0 (CC BY).

PMC Copyright notice

(A) In vitro interaction of STK38 kinases with HEY1. Whole-cell extracts from U2OS cells previously transfected with expression vectors for V5-tagged HEY1 were incubated with Flag-tagged-STK38 or STK38L coupled with anti-Flag magnetic beads. The associated proteins were detected by western blotting using anti-V5 antibody. (B) HEY1 is phosphorylated at serine 68 in vitro by okadaic acid-activated STK38 and STK38L kinases. U2OS cells expressing Flag-tagged STK38 or STK38L kinases were incubated for 1 h with vehicle or 1 μM okadaic acid. Flag-tagged kinases were then immunoprecipitated and assayed for kinase activity using immunopurified FLAG-tagged wild-type HEY1 or the non-phosphorylatable HEY1-S68A mutant as substrate. Phosphorylation of HEY1 was determined by western blotting with anti-phospho-S68 antibody. Western blotting with anti-Flag antibody shows the amount of Flag-HEY1, Flag-STK38 or Flag-STK38L present in each assay.