Program

Oral Sessions

Day 4, May 18（Fri.）　09:20-09:40　Room A (OrBit Hall)

4A-O1-P-0920　　PDF

Phosphorylation Network Analysis Based on Kinome Profiling

(Kyoto Univ.)
^oNaoyuki Sugiyama, Haruna Imamura, Dai Sakamoto, Junna Nakazono, Kazutaka Yachigo, Chisato Takahashi, Hsin-yi Chang, Yasushi Ishihama

Protein phosphorylation mediated by protein kinases is important for cellular signal transduction networks. Large-scale phosphoproteomics enables us to overview protein phosphorylation events in the cell signaling. Recently, large-scale phosphoproteomics based on LC-MS/MS and phosphopeptide-selective enrichment has become a powerful tool to reveal the signaling mechanisms. However, it is still challenge to clarify a role and regulation mechanism of individual kinase from the phosphoproteome analysis since crosstalk between signaling pathways is complicated and kinase-substrate relationships have not been completely cleared yet. Here, we profiled more than 400 recombinant human kinases by using in vitro kinase assay combined with quantitative phosphoproteomics approaches. We also designed kinase-specific substrate peptides and developed a method for direct monitoring of kinase activities at the kinome-wide scale.