液―液相分離が維持するCaMKIIの分子活性

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  • Persistence of CaMKII activity in liquid condensates

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<p>Liquid-liquid phase separation (LLPS) is a phenomenon in which different proteins spontaneously assemble within a cellular compartment that recognized as a membraneless organelle. LLPS plays important roles in neurons, particularly in the structural organization of postsynaptic densities.</p><p>Calmodulin-dependent protein kinase II (CaMKII) is a major synaptic protein kinase and a key regulator of synaptic plasticity. CaMKII forms calcium-gated condensates with the glutamate receptor subunit GluN2B via LLPS. Since the interaction with GluN2B maintains CaMKII in an active conformation, we hypothesize that the LLPS of CaMKII serves as a molecular machine to maintain biochemical activity as a memory. Given that a protein in a liquid condensate can be replaced by an external protein, a protein cannot persist in the condensate for long time, but the condensate itself can persist for a long time. This unique property reasonably explains how the condensate of CaMKII can be a memory unit that lasts longer than the lifetime of the protein. </p><p>In this symposium, I will present our recent progress on how CaMKII maintains its activity at the synapse using the in vitro reconstituted LLPS assay and nanobody-assisted synaptic translocation of CaMKII into the synapse combined with the FRET sensor of CaMKII.</p>

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