| Project/Area Number |
16K14583
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Neurochemistry/Neuropharmacology
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| Research Institution | Waseda University |
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Principal Investigator |
Akiyama Hiroki 早稲田大学, 人間科学学術院, 講師(任期付) (40568854)
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| Project Period (FY) |
2016-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2016: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | SUMO / SENP / SUMO化 / SENP5 / シナプス / 神経突起 / シナプス伝達 |
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| Outline of Final Research Achievements |
Covalent conjugation of small ubiquitin-like modifiers (SUMOs) or SUMOylation is a reversible post-translational modification that regulates the stability and function of target proteins. Numerous studies have implicated SUMOylation in various physiological and pathological processes in cells and organs; however, SUMOylation-regulating machinery remains elusive. The balance between ligase-mediated conjugation and protease-mediated deconjugation is regarded as a determinant of SUMOylation state of target proteins. We identified a novel isoform of sentrin/SUMO-specific protease 5 (SENP5, referred to as SENP5S) that lacks the catalytic domain. Expression of SENP5S increased the amount of SUMOylated proteins, likely by competing with endogenous SENPs. This finding demonstrates a novel mechanism by which SUMO-interacting molecule like SENP5S can modulate SUMOylation state of target proteins in an enzymatic activity-independent manner.
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