Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation
Dynamic control of CaMKII translocation and localization in hippocampal neurons by NMDA receptor stimulation
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DOI：
10.1126/science.284.5411.162
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发表时间：
1999-04-02
期刊：
影响因子：
56.9
通讯作者：
Meyer, T
中科院分区：
文献类型：
--
作者：
Shen, K;Meyer, T
钙-钙调素依赖性蛋白激酶II （CaMKII）被认为通过磷酸化突触后密度（PSD）离子通道和信号蛋白来增加突触强度。研究表明，n-甲基- d -天冬氨酸（NMDA）受体刺激可将绿色荧光蛋白标记的CaMKII从f -actin结合状态可逆地转运到psd结合状态。易位时间由表达的β - camkii与α - camkii异构体的比例控制。虽然f -肌动蛋白解离到细胞质中需要钙-钙调蛋白与β - camkii结合的自磷酸化，但PSD易位需要钙-钙调蛋白与α -或β - camkii亚基结合。CaMKII的自磷酸化通过增加钙调素结合亲和力间接延长了其PSD定位。
Calcium-calmodulin-dependent protein kinase II (CaMKII) is thought to increase synaptic strength by phosphorylating postsynaptic density (PSD) ion channels and signaling proteins. It is shown that N-methyl-D-aspartate (NMDA) receptor stimulation reversibly translocates green fluorescent protein-tagged CaMKII from an F-actin-bound to a PSD-bound state. The translocation time was controlled by the ratio of expressed beta-CaMKII to alpha-CaMKII isoforms. Although F-actin dissociation into the cytosol required autophosphorylation of or calcium-calmodulin binding to beta-CaMKII, PSD translocation required binding of calcium-calmodulin to either the alpha- or beta-CaMKII subunits. Autophosphorylation of CaMKII indirectly prolongs its PSD localization by increasing the calmodulin-binding affinity.