Molecular determinants of NMDA receptor internalization

被引:414
|
作者
Roche, KW
Standley, S
McCallum, J
Ly, CD
Ehlers, MD
Wenthold, RJ
机构
[1] Natl Inst Deafness & Other Commun Disorders, Neurochem Lab, NIH, Bethesda, MD 20892 USA
[2] Duke Univ, Med Ctr, Dept Neurobiol, Durham, NC 27710 USA
关键词
D O I
10.1038/90498
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Although synaptic AMPA receptors have been shown to rapidly internalize, synaptic NMDA receptors are reported to be static. It is not certain whether NMDA receptor stability at synaptic sites is an inherent property of the receptor, or is due to stabilization by scaffolding proteins. In this study, we demonstrate that NMDA receptors are internalized in both heterologous cells and neurons, and we define an internalization motif, YEKL, on the distal C-terminus of NR2B. In addition, we show that the synaptic protein PSD-95 inhibits NR2B-mediated internalization, and that deletion of the PDZ-binding domain of NR2B increases internalization in neurons. This suggests an involvement for PSD-95 in NMDA receptor regulation and an explanation for NMDA receptor stability at synaptic sites.
引用
收藏
页码:794 / 802
页数:9
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