PHOSPHOPROTEOMICS TO STUDY KINASE INHIBITOR ACTION

Protein kinases are important mediators of intracellular signaling and exert their function via the posttranslational addition of a phosphate group to serine, threonine or tyrosine residues. As aberrant kinase activity is often associated with proliferative diseases like cancer, kinases are prime targets for the design of small molecule inhibitors.

An HPLC based Fe-IMAC column method established in our lab enables us to comprehensively purify phosphopeptides out of complex lysates. Coupled to mass spectrometry we are able to quantitatively monitor >10.000 phosphorylation events simultaneously from cancer cells or tumor tissue. The project focus is directed towards the better understanding of the cancer phosphoproteome to identify potential novel drug targets and signaling biomarkers able to indicate response to therapy.