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Poster Presentations
Day 3, June 24（Tue.）
Room P (Maesato East, Foyer, Ocean Wing)
- 3P-AM-49（2B-O1-1155）
Phosphatase reactivity-based profiling of the local environment of phosphorylation sites on proteins
(1Kyoto Univ., 2NIBIOHN)
oYuna Hiranuma1, Kosuke Ogata1, Yasushi Ishihama1,2
Proving the structural state of each phosphosite is necessary to understand its function. However, conventional structural analysis methods are not effective for analyzing phosphosites. In this study, we aimed to develop a phosphosite profiling method that combines an in vitro phosphatase dephosphorylation reaction with mass spectrometry to characterize the local environment of specific phosphosites based on reaction efficiency. We applied this method to profiling human recombinant Bruton's tyrosine kinase (BTK) and identified phosphosites that showed altered reaction efficiency upon denaturation by urea. The results show that the dephosphorylation efficiency reflects the structure and the structural changes around each phosphosite under different urea concentrations.