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

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.

Pubmed ID: 12738960


  • Sans N
  • Prybylowski K
  • Petralia RS
  • Chang K
  • Wang YX
  • Racca C
  • Vicini S
  • Wenthold RJ


Nature cell biology

Publication Data

June 30, 2003

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Brain Chemistry
  • COS Cells
  • Carrier Proteins
  • Cells, Cultured
  • Cercopithecus aethiops
  • Exocytosis
  • Models, Biological
  • Molecular Sequence Data
  • Mutation
  • Neurons
  • Neuropeptides
  • Protein Binding
  • Protein Transport
  • Rats
  • Receptors, N-Methyl-D-Aspartate