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Poster Presentations
Day 4, June 25（Wed.）
Room P (Maesato East, Foyer, Ocean Wing)
- 4P-AM-22
Quantitative Proteomics of Post-Translational Modification in Parkinson's Disease Model Cells
(Yokohama City Univ.)
oShunsuke Hoshina, Eri Katsuno, Daisuke Takakura, Tohru Sugawara, Nana Kawasaki
Post-translational modifications of proteins, including O-N-Acetylglucosaminylation (O-GlcNAcylation) and phosphorylation involved in signal transduction, function in various biological phenomena and the onset of diseases. O-GlcNAcylation is known to be associated with Parkinson's disease (PD)2,3 through changing phosphorylation. It is important to clarify the relationship between O-GlcNAcylation and phosphorylation in PD to elucidate the mechanism underlying PD and develop modalities. In this study, we aimed to generate PD models from induced pluripotent stem cells (iPSCs) and conduct a differential analysis of O-GlcNAcylation and phosphorylation between PD models and wild type (WT) using DIA-MS. Spectral libraries of 154 O-GlcNAcylated peptides from 57 proteins and 18151 phosphorylated peptides of 5178 proteins were constructed to implement differential analysis with DIA-MS. Notably, O-GlcNAcylated peptides from nuclear envelope pore membrane protein POM 121C (POM121C) and nuclear pore complex protein Nup153 (Nup153) showed decreased expression in PD-dopaminergic neurons (DA). Phosphoproteomics revealed the increase in phosphorylation of POM121C and Nup153 in PD-DA. Abnormalities in nuclear envelope morphology have been reported in Neural stem cells derived from iPSCs from PD patients with LRRK2 mutations. Reduced O-GlcNAcylation may promote phosphorylation of the proteins and causes deformation of the nuclear envelope in PD with LRRK2 mutation.