| Budget Amount *help |
¥146,380,000 (Direct Cost: ¥112,600,000、Indirect Cost: ¥33,780,000)
Fiscal Year 2016: ¥11,180,000 (Direct Cost: ¥8,600,000、Indirect Cost: ¥2,580,000)
Fiscal Year 2015: ¥18,980,000 (Direct Cost: ¥14,600,000、Indirect Cost: ¥4,380,000)
Fiscal Year 2014: ¥11,310,000 (Direct Cost: ¥8,700,000、Indirect Cost: ¥2,610,000)
Fiscal Year 2013: ¥11,180,000 (Direct Cost: ¥8,600,000、Indirect Cost: ¥2,580,000)
Fiscal Year 2012: ¥93,730,000 (Direct Cost: ¥72,100,000、Indirect Cost: ¥21,630,000)
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| Outline of Final Research Achievements |
Ubiquitylation is a post-translational modification that regulates numerous important cellular processes including proteasomal degradation, DNA repair, protein sorting, and signal transduction. The diverse functions of ubiquitin depend on the ubiquitin chain topology with eight linkage types, lengths, chemical modifications, and their combinations. To clarify the ubiquitin code, we developed an ultra-sensitive absolute quantification method of ubiquitin chains and a comprehensive identification method of ubiquitylated substrates using a high resolution mass spectrometry. Then, we applied them to the analysis of various important substrates found in the research group. In addition, we comprehensively analyzed ubiquitin chain type selectivity of yeast ubiquitin-binding proteins and found that proteasomal degradation is predominantly regulated by the Cdc48-Rad23/Dsk2 axis. Thus, we provided the first overall picture of the ubiquitin network via ubiquitin-binding proteins.
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