Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation
Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation
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DOI：
10.1126/science.276.5321.2042
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发表时间：
1997-06-27
期刊：
影响因子：
56.9
通讯作者：
Soderling, TR
中科院分区：
文献类型：
--
作者：
Barria, A;Muller, D;Soderling, TR
长期增强（LTP）是一种学习和记忆的细胞模型，需要钙依赖性蛋白激酶。LTP的诱导增加了介导快速兴奋性突触传递的α -氨基-3-羟基-5-甲基-4-异唑丙酸（AMPA）型谷氨酸受体（AMPA- rs）的磷-32标记。这种AMPA-R磷酸化似乎是由Ca2+和钙调素依赖性蛋白激酶II （CaM-KII）催化的：(i)它与CaM-KII的活化和自磷酸化相关，（II）它被CaM-KII抑制剂k -62阻断，（iii）它的磷酸化-32肽图与HEK-293细胞中与活化的CaM-KII共表达的GluR1相同。LTP中AMPA-Rs的共价调控为突触可塑性提供了一种突触后分子机制。
Longterm potentiation (LTP), a cellular model of learning and memory, requires calcium-dependent protein kinases. Induction of LTP increased the phosphorus-32 labeling of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPA-Rs), which mediate rapid excitatory synaptic transmission. This AMPA-R phosphorylation appeared to be catalyzed by Ca2+- and calmodulin-dependent protein kinase II (CaM-KII): (i) it correlated with the activation and autophosphorylation of CaM-KII, (ii) it was blocked by the CaM-KII inhibitor KN-62, and (iii)its phosphorus-32 peptide map was the same as that of GluR1 coexpressed with activated CaM-KII in HEK-293 cells. This covalent modulation of AMPA-Rs in LTP provides a postsynaptic molecular mechanism for synaptic plasticity.