Driving AMPA receptors into synapses by LTP and CaMKII: Requirement for GluR1 and PDZ domain interaction
Driving AMPA receptors into synapses by LTP and CaMKII: Requirement for GluR1 and PDZ domain interaction
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DOI：
10.1126/science.287.5461.2262
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发表时间：
2000-03-24
期刊：
影响因子：
56.9
通讯作者：
Malinow, R
中科院分区：
文献类型：
--
作者：
Hayashi, Y;Shi, SH;Malinow, R
为了阐明控制和执行活动依赖性突触可塑性的机制，在大鼠海马神经元中表达具有电生理标签的α-氨基-3-羟基-5-甲基-4-异恶唑丙酸酯受体（AMPA-Rs）。长时程增强（LTP）或钙/钙调蛋白依赖性蛋白激酶II（CaMKII）活性增加诱导的标签AMPA-R传递到突触。这种作用并没有通过突变GLuR 1 AMPA-R亚基上的CaMKII磷酸化位点而减弱，但通过突变预测的PDZ结构域相互作用位点而被阻断。这些结果表明，LTP和CaMKII活性驱动AMPA-R突触的机制，需要之间的关联GluR 1和PDZ结构域蛋白。
To elucidate mechanisms that control and execute activity-dependent synaptic plasticity, alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptors (AMPA-Rs) with an electrophysiological tag were expressed in rat hippocampal neurons. Long-term potentiation (LTP) or increased activity of the calcium/calmodulin-dependent protein kinase II (CaMKII) induced delivery of tagged AMPA-Rs into synapses. This effect was not diminished by mutating the CaMKII phosphorylation site on the GLuR1 AMPA-R subunit, but was blocked by mutating a predicted PDZ domain interaction site. These results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein.