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

Authors: Sans, N  Prybylowski, K  Petralia, RS  Chang, K  Wang, YX  Racca, C  Vicini, S  Wenthold, RJ 
Citation: Sans N, etal., Nat Cell Biol. 2003 Jun;5(6):520-30.
Pubmed: (View Article at PubMed) PMID:12738960
DOI: Full-text: DOI:10.1038/ncb990

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.

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CRRD Object Information
CRRD ID: 8554028
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.