Crosstalk among the proteome, lysine phosphorylation, and acetylation in romidepsin-treated colon cancer cells.

ABSTRACT: Romidepsin (FK228) is one of the most promising histone-deacetylase inhibitors due to its potent antitumor activity, and has been used as a practical option for cancer therapy. However, FK228-induced changes in protein modifications and the crosstalk between different modifications has not been reported. To better understand the underlying mechanisms of FK228-related cancer therapy, we investigated the acetylome, phosphorylation, and crosstalk between modification datasets in colon cancer cells treated with FK228 by using stable-isotope labeling with amino acids in cell culture and affinity enrichment, followed by high-resolution liquid chromatography tandem mass spectrometry analysis. In total, 2728 protein groups, 1175 lysine-acetylation sites, and 4119 lysine-phosphorylation sites were

SUBMITTER: Wang TY 

PROVIDER: S-EPMC5288200 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature