The role of phosphorylation in F-actin binding domain of CaMKII in structural and functional plasticity

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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.