2017 Fiscal Year Final Research Report
HS-AFM studies of molecular mechanisms of learning and memory in CaMKII oligomer
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 |
Research Field |
Biophysics
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Research Institution | Kanazawa University |
Principal Investigator |
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Project Period (FY) |
2016-04-01 – 2018-03-31
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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 |
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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Free Research Field |
生物物理学
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