DOMAIN INTERACTION BETWEEN NMDA RECEPTOR SUBUNITS AND THE POSTSYNAPTIC DENSITY PROTEIN PSD-95
DOMAIN INTERACTION BETWEEN NMDA RECEPTOR SUBUNITS AND THE POSTSYNAPTIC DENSITY PROTEIN PSD-95
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DOI：
10.1126/science.7569905
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发表时间：
1995-09-22
期刊：
影响因子：
56.9
通讯作者：
SEEBURG, PH
中科院分区：
文献类型：
--
作者：
KORNAU, HC;SCHENKER, LT;SEEBURG, PH
N-甲基-D-天冬氨酸(NMDA)受体参与突触谷氨酸诱导的中枢神经元传递和可塑性。酵母双杂交系统显示NMDA受体亚基的细胞质尾巴与突触后密度蛋白PSD-95相互作用。PSD-95中的第二个PDZ结构域与七个氨基酸的COOH-末端结构域结合，该结构域包含NR2亚基共有的末端TSXV基序(其中S为丝氨酸，X为任何氨基酸，V为缬氨酸)和某些NR1剪接形式。编码PSD-95的转录本以类似于NMDA受体的模式表达，在培养的大鼠海马神经元中，NR2B亚单位与PSD-95共定位。这些蛋白的相互作用可能影响兴奋性突触的可塑性。
The N-methyl-D-aspartate (NMDA) receptor subserves synaptic glutamate-induced transmission and plasticity in central neurons. The yeast two-hybrid system was used to show that the cytoplasmic tails of NMDA receptor subunits interact with a prominent postsynaptic density protein PSD-95. The second PDZ domain in PSD-95 binds to the seven-amino acid, COOH-terminal domain containing the terminal tSXV motif (where S is serine, X is any amino acid, and V is valine) common to NR2 subunits and certain NR1 splice forms. Transcripts encoding PSD-95 are expressed in a pattern similar to that of NMDA receptors, and the NR2B subunit co-localizes with PSD-95 in cultured rat hippocampal neurons. The interaction of these proteins may affect the plasticity of excitatory synapses.