Kornau H C, Schenker L T, Kennedy M B, Seeburg P H
Center for Molecular Biology (ZMBH), University of Heidelberg, Germany.
Science. 1995 Sep 22;269(5231):1737-40. doi: 10.1126/science.7569905.
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.
N-甲基-D-天冬氨酸（NMDA）受体在中枢神经元中参与突触谷氨酸诱导的传递和可塑性。利用酵母双杂交系统表明，NMDA受体亚基的胞质尾与一种突出的突触后致密蛋白PSD-95相互作用。PSD-95中的第二个PDZ结构域与包含NR2亚基和某些NR1剪接形式共有的末端tSXV基序（其中S是丝氨酸，X是任何氨基酸，V是缬氨酸）的七氨基酸COOH末端结构域结合。编码PSD-95的转录本以与NMDA受体相似的模式表达，并且NR2B亚基在培养的大鼠海马神经元中与PSD-95共定位。这些蛋白质的相互作用可能影响兴奋性突触的可塑性。
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