Phosphoproteomic and Acetylomic Characterization of Colorectal Cancer Cells Treated with Kinase Inhibitors

Kinase inhibitors have long been
studied to be developed
into therapeutic
drugs or chemical probes, but their off-target effects in phosphoproteomics
and acetylomics remain largely unexplored. Here, we provided a systematic
molecular response to kinase inhibitors in the colorectal cancer cell
line, including the proteomics, phosphoproteomics, and acetylomics.
The results provided comprehensive kinase activity perturbations of
each kinase inhibitor and presented unique pathway-level biological
effects, mitochondrial functional perturbations, and kinase activity
changes for inhibitors targeting the same pathway. Furthermore, we
discovered the potential protein post-translational modification (PTM)
crosstalk between lysine acetylation and protein phosphorylation.
The study additionally proposed potential combination treatment strategies.
In summary, this study presented in-depth and comprehensive analysis
results of kinase inhibitor perturbations on the colorectal cancer
cell line at proteomic, phosphoproteomic, and acetylomic landscapes.