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. 2018 Jul 3;9(7):747. doi: 10.1038/s41419-018-0774-8

Fig. 5. Activation of PP2A induced degradation of YY1 protein.

Fig. 5

a Okadaic acid slightly upregulated YY1 promoter activity. CAL27 cells transfected with YY1 promoter plasmid and treated with okadaic acid or not for 24 h. Total proteins were extracted and subjected to luciferase assay and normalized by total protein concentration. t-test, *P < 0.05 (n = 9). b, c Okadaic acid slightly upregulated YY1 mRNA but significantly upregulated YY1 protein expression. CAL27 cells were exposed to okadaic acid for 48 h, mRNA expression was quantitated by real-time PCR, one-way ANOVA: *P < 0.05 (n = 3) b; total protein was subjected to Western blot analysis c, t-test, *P < 0.05 (n = 3). d Forskolin slightly downregulated YY1 promoter activity. CAL27 cells transfected with YY1 promoter plasmid and treated with forskolin or not for 24 h. Total protein was subjected to luciferase assay and normalized by total protein concentration. t-test, *P < 0.05 (n = 9). e, f Forskolin slightly downregulated YY1 mRNA but significantly downregulated YY1 protein expression. CAL27 cells were treated with forskolin for 48 h, mRNA expression was quantitated by real-time PCR, one-way ANOVA: *P < 0.05, n = 3 (e); total protein was subjected to Western blot analysis, t-test, *P < 0.05, n = 3 (f). g Forskolin induced ubiquitination of YY1 expression. 293 T cells were transfected with HA-ubiquitin or GFP-YY1 or both and transfected cells were exposed to forskolin or not for 48 h. Whole-cell lysates were immunoprecipitated with GFP antibody and the immunocomplexes were subjected to Western blot with HA antibody. c, f The target bands were exposed, and densitometry was performed as fold change ratio from the mean of three independent experiments, t-test, *P < 0.05. (Bars: mean ± SD)