STIMULATION OF PROTEIN TYROSINE PHOSPHORYLATION BY NMDA RECEPTOR ACTIVATION
STIMULATION OF PROTEIN TYROSINE PHOSPHORYLATION BY NMDA RECEPTOR ACTIVATION
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DOI：
10.1126/science.1715095
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发表时间：
1991-08-23
期刊：
影响因子：
56.9
通讯作者：
GREENBERG, ME
中科院分区：
文献类型：
--
作者：
BADING, H;GREENBERG, ME
N-甲基-D-天冬氨酸（NMDA）受体是谷氨酸受体的一种亚型，在神经系统的突触可塑性中起着关键作用。NMDA受体激活后，钙离子进入突触后神经元是一个关键的初始事件。然而，NMDA受体信号处理的后续机制尚未完全了解。用谷氨酸刺激培养的大鼠海马细胞导致39千道尔顿蛋白（p39）的快速和短暂的酪氨酸磷酸化。p39的酪氨酸磷酸化是由NMDA受体触发的，并且需要来自细胞外介质的Ca 2+的流入。因为p39被发现是高度相关或相同的微管相关蛋白2激酶，NMDA受体信号可能是由蛋白激酶的顺序激活处理。
The N-methyl-D-aspartate (NMDA) receptor, a subtype of glutamate receptors, plays a key role in synaptic plasticity in the nervous system. After NMDA receptor activation, calcium entry into the postsynaptic neuron is a critical initial event. However, the subsequent mechanisms by which the NMDA receptor signal is processed are incompletely understood. Stimulation of cultured rat hippocampal cells with glutamate resulted in the rapid and transient tyrosine phosphorylation of a 39-kilodalton protein (p39). Tyrosine phosphorylation of p39 was triggered by the NMDA receptor and required an influx of Ca2+ from the extracellular medium. Because p39 was found to be highly related or identical to the microtubule-associated protein 2 kinase, the NMDA receptor signal may be processed by a sequential activation of protein kinases.