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. 2018 May 7;115(21):5546–5551. doi: 10.1073/pnas.1719856115

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Fig. 1. — USP3 regulates BTG3-promoted CHK1 ubiquitination. (A) The ubiquitinated CHK1 lost its catalytic activity. The in vitro kinase assay was performed with unmodified CHK1 or ubiquitinated CHK1 immunoprecipitated from 293T cells coexpressing or not coexpressing BTG3, using GST-Cdc25C_200–256 as the substrate. (B) USP3 down-regulation increased BTG3-promoted CHK1 ubiquitination. RT-PCR was used to confirm the knockdown. SC, scramble control siRNA. (C and D) Down-regulation of USP3 increased UV-induced CHK1 activation (pS345) in HCT116 (C) and 293T (D) cells. (E and F) UV-induced CHK1 S345 phosphorylation was diminished by USP3 overexpression in HCT116 (E) and 293T (F) cells.