The role of phosphorylation in F-actin binding domain of CaMKII in structural and functional plasticity
| Project/Area Number |
22700356
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Neuroscience in general
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
KIM Karam 独立行政法人理化学研究所, 記憶メカニズム研究チーム, 研究員 (60568856)
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| Project Period (FY) |
2010 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2011: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2010: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | CaMKII / シナプス可塑性 / アクチン / スパイン / 海馬 / spine / LTP / phosphorylation / Actin Bundling / Actin modification |
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| Research Abstract |
In this project, we identified 18 new phosphorylation sites in actin-binding domain of CaMKIIβ. They are phosphorylated via inter-subunit manner and their phosphorylation is important in spine localization and F-actin bundling of CaMKIIβ. Using biochemical methods, we showed that CaMKIIβ-mediated F-actin bundling stabilizes F-actin and it inhibits the not only interactions between actin and its regulator proteins, but also their activities against actin. It has in vivo relevance so that phosphor-resistant mutant form of CaMKIIβsuppresses both enlargement of a spine induced by glutamate uncaging and LTP measured with electrophysiological method in rat hippocampal slices.
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Report
(3 results)
Research Products
(6 results)
