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CaMKIIα-driven, phosphatase-checked postsynaptic plasticity via phase separation
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CaMKIIα-driven, phosphatase-checked postsynaptic plasticity via phase separation
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Journal Article
CaMKIIα-driven, phosphatase-checked postsynaptic plasticity via phase separation
2021
Overview
Ca
2+
/calmodulin-dependent kinase IIα (CaMKIIα) is essential for synaptic plasticity and learning by decoding synaptic Ca
2+
oscillations. Despite decades of extensive research, new mechanisms underlying CaMKIIα’s function in synapses are still being discovered. Here, we discover that Shank3 is a specific binding partner for autoinhibited CaMKIIα. We demonstrate that Shank3 and GluN2B, via combined actions of Ca
2+
and phosphatases, reciprocally bind to CaMKIIα. Under basal condition, CaMKIIα is recruited to the Shank3 subcompartment of postsynaptic density (PSD) via phase separation. Rise of Ca
2+
concentration induces GluN2B-mediated recruitment of active CaMKIIα and formation of the CaMKIIα/GluN2B/PSD-95 condensates, which are autonomously dispersed upon Ca
2+
removal. Protein phosphatases control the Ca
2+
-dependent shuttling of CaMKIIα between the two PSD subcompartments and PSD condensate formation. Activation of CaMKIIα further enlarges the PSD assembly and induces structural LTP. Thus, Ca
2+
-induced and phosphatase-checked shuttling of CaMKIIα between distinct PSD nano-domains can regulate phase separation-mediated PSD assembly and synaptic plasticity.
Publisher
Springer Singapore,Nature Publishing Group
Subject
/ 631/80
/ 82
/ Animals
/ Assembly
/ Biomedical and Life Sciences
/ Calcium-Calmodulin-Dependent Protein Kinase Type 2 - chemistry
/ Calcium-Calmodulin-Dependent Protein Kinase Type 2 - genetics
/ Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism
/ Disks Large Homolog 4 Protein - genetics
/ Disks Large Homolog 4 Protein - metabolism
/ Humans
/ Kinases
/ Mice
/ Molecular Docking Simulation
/ Nerve Tissue Proteins - chemistry
/ Nerve Tissue Proteins - metabolism
/ Neuronal Plasticity - physiology
/ Phosphoprotein Phosphatases - metabolism
/ Postsynaptic density proteins
/ Rats
/ Receptors, N-Methyl-D-Aspartate - genetics
/ Receptors, N-Methyl-D-Aspartate - metabolism
/ SAP90-PSD95 Associated Proteins - metabolism
/ Synapses
