Fig. 5
From: STK16 promoted colorectal cancer progress in a c-MYC signaling-dependent manner
STK16 Phosphorylated c-MYC at Serine 452. A. IB and immunoprecipitation (IP) assays confirmed the binding of STK16 and c-MYC. B. IB and IP assays assessed the phosphorylation level of c-MYC in RKO cells stably expressing vector, STK16 WT, or STK16 H198A. C. IB and IP assays assessed the phosphorylation level of c-MYC in RKO cells stably expressing sgCtrl or sgSTK16. D, E. IB and IP assays investigated the binding domain of STK16 and c-MYC. F. Transfected c-MYC S430A or c-MYC S452A mutant plasmid into HEK293T cells, and IB and IP assays assessed the phosphorylation level of c-MYC in HEK293T cells stably expressing vector or STK16. G. IB and IP assays assessed the poly-ubiquitination level of c-MYC WT, c-MYC S452A, or c-MYC S452E. H. IB assays assessed the expression of c-MYC signaling-related proteins in cancer cells stably expressing c-MYC WT, c-MYC S452A, or c-MYC S452E. I-K. CCK8 (I) and Brdu (J, K) assays assessed the proliferation ability of cancer cells stably expressing c-MYC WT, c-MYC S452A, or c-MYC S452E. All IB assays were conducted three times, and consistent results were obtained. Statistical analysis used Student’s t-test