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. 2020 Feb 10;9(2):15. doi: 10.1038/s41389-020-0195-2

Fig. 6. MSK1 and STAT3 can be recruited to the promoter of NFATC2, and activate its expression by coupling histone phosphorylation.

Fig. 6

a, b STAT3 and MSK1 protein interaction was derived from HEK 293T cells following the transfection with Myc-MSK1 and Flag-STAT3 by immunoprecipitation assay (IP). c Endogenous interaction between Stat3 and MSK1 by IP analysis derived from GES-1 or MNNG-transformed cells. d Flag-STAT3 fragments were co-expressed with Myc-MSK1 wild-type in HEK293T cells. After anti-Myc immunoprecipitation, coprecipitated STAT3 was revealed by immunoblotting. e RT-qPCR analysis of NFATc2 mRNA expression after STAT3 overexpression or siRNA knockdown. f The binding of MSK1 (left) or STAT3 (right) to the promoter of NFATc2 was analyzed by ChIP assay with anti-MSK1 or anti-STAT3 antibody in the MNNG-transformed cells treated with vehicle or AG490. Ctr: control site. MSK1-BS: MSK1 binding site. STAT3-BS1: STAT3 binding site 1. STAT3-BS2: STAT3 binding site 2. g The correlation between STAT3 and NFATc2 expression or MSK1 and NFATc2 expression of the TCGA database were analyzed by GEPIA. The analyses were repeated three times, and the results were expressed as mean ± SD. *p < 0.05 and ##p < 0.01.