NMDA receptor trafficking through an interaction between PDZ proteins and the exocyst complex

被引：249

作者：

Sans, N

Prybylowski, K

Petralia, RS

Chang, K

Wang, YX

Racca, C

Vicini, S

Wenthold, RJ

机构：

[1] Natl Inst Deafness & Other Commun Disorders, Neurochem Lab, NIH, Bethesda, MD 20892 USA

[2] Georgetown Univ, Dept Physiol & Biophys, Med Ctr, Washington, DC 20057 USA

来源：

NATURE CELL BIOLOGY | 2003年 / 5卷 / 06期

关键词：

D O I：

10.1038/ncb990

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

NMDA (N-methyl-D-aspartate) receptors (NMDARs) are targeted to dendrites and anchored at the post-synaptic density (PSD) through interactions with PDZ proteins. However, little is known about how these receptors are sorted from the endoplasmic reticulum and Golgi apparatus to the synapse. Here, we find that synapse-associated protein 102 (SAP102) interacts with the PDZ-binding domain of Sec8, a member of the exocyst complex. Our results show that interactions between SAP102 and Sec8 are involved in the delivery of NMDARs to the cell surface in heterologous cells and neurons. Furthermore, they suggest that an exocyst-SAP102-NMDAR complex is an important component of NMDAR trafficking.

引用

页码：520 / 530

页数：11

共 47 条

[21] Cloning and characterization of NE-dlg: A novel human homolog of the Drosophila discs large (dlg) tumor suppressor protein interacts with the APC protein [J].