Activated CaMKII couples GluN2B and casein kinase 2 to control synaptic NMDA receptors.
Activated CaMKII couples GluN2B and casein kinase 2 to control synaptic NMDA receptors.
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DOI：
10.1016/j.celrep.2013.02.011
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发表时间：
2013-03-28
期刊：
影响因子：
8.8
通讯作者：
Roche KW
中科院分区：
文献类型：
--
作者：
Sanz-Clemente A;Gray JA;Ogilvie KA;Nicoll RA;Roche KW
Synaptic activity triggers a profound reorganization of the molecular composition of excitatory synapses. For example, NMDA receptors are removed from synapses in an activity- and calcium-dependent manner, via casein kinase 2 (CK2) phosphorylation of the PDZ-ligand of the GluN2B subunit (S1480). However, how synaptic activity drives this process remains unclear because CK2 is a constitutively active kinase, which is not directly regulated by calcium. We show here that activated CaMKII couples GluN2B and CK2 to form a tri-molecular complex and increase CK2-mediated phosphorylation of GluN2B S1480. In addition, a GluN2B mutant, which contains an insert to mimic the GluN2A sequence and cannot bind to CaMKII, displays reduced S1480 phosphorylation and increased surface-expression. Importantly, we find that although disrupting GluN2B/CaMKII binding reduces synapse number, it increases synaptic-GluN2B content. Therefore, the GluN2B/CaMKII association controls synapse density and PSD composition in an activity-dependent manner, including recruitment of CK2 to remove GluN2B from synapses.
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DOI：
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发表时间：
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期刊：
Journal of visualized experiments : JoVE
影响因子：
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