- 第3日 5月17日（木） 09:30～09:45 B会場（星雲1）
Protein phosphorylation catalyzed by kinases is one of the most ubiquitous post-translational modifications and plays significant roles in cellular signal transduction. Monitoring kinome activities provides us an understanding of the cellular signaling network, and can be beneficial for the diagnosis. Although phosphoproteomics based on LC/MS/MS enables us to identify a large number of phosphosites, these data lack the information of responsible kinases. Thus, it is difficult to measure kinome activities by current phosphoproteomics approaches. In this study, we developed a method to monitor kinome activities using kinase-specific substrate peptides.