Fig. 5: Acetylation of CHES1 enhanced its protein stability via decreasing its ubiquitination. | Cell Death Discovery

Fig. 5: Acetylation of CHES1 enhanced its protein stability via decreasing its ubiquitination.

From: Acetylation of Checkpoint suppressor 1 enhances its stability and promotes the progression of triple-negative breast cancer

Fig. 5

A The effect of HDACs inhibitors on the protein levels of exogenous CHES1. B Western blot showed the half-life of wild type CHES1 and its KR mutant after treating with 10 μg/ml CHX. The line graph showed the relative intensity of CHES1 protein levels in different time normalized by β-actin, ***p＜0.001. C IP assay showed the polyubiquitination levels of wild type CHES1 and its KR mutant with or without treatment of 20 μg/ml MG132 for 6 h. D IP assay detected the acetylation and ubiquitination of endogenous CHES1 in different types of breast cancer cells pretreated with TSA and NAM. “*” denotes the non-specific band. E CoIP assay showed the endogenous interaction between CHES1 and HDAC1 in MCF7 and MDA-MB-231 cells.

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