| Project/Area Number |
16K18523
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biophysics
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| Research Institution | Kanazawa University |
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Principal Investigator |
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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 |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2017: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2016: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | タンパク質 / 記憶 / プロテインキナーゼ / 走査型プローブ顕微鏡 / 原子間力顕微鏡 / 高速原子間力顕微鏡 / 神経科学 / ナノサイエンス / バイオイメージング / 生物物理 / 走査プローブ顕微鏡 / ナノバイオ |
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| Outline of Final Research Achievements |
CaMKII is enriched in neurons and plays an important role for learning and memory. Because CaMKII forms 12-mer holoenzyme that responds to the frequency of the activating signal of Ca2+, an assembly of CaMKII oligomers could be a key element of a molecular mechanism of learning and memory. However, there is no direct evidence that a formation of CaMKII oligomer relates to a memory mechanism.
HS-AFM movies of CaMKII showed solid structures and fluctuated globular structures. By using truncated CaMKII, solid and globular structures were assigned to hub and kinase domains, respectively. Interestingly, 14-mer ring structures were observed in the truncated CaMKII, while 12-mer structures were observed in full-length CaMKII. These results suggest that hub domain has a strong assemble ability, while kinase domain regulates an oligomeric structure of CaMKII. Furthermore, HS-AFM revealed that a flexibility of a linker region is important for the activation of CaMKII.
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