Glutamate receptor anchoring proteins and the molecular organization of excitatory synapses.
Ionotropic glutamate receptors are concentrated at postsynaptic sites in excitatory synapses. The cytoplasmic C-terminal tail of certain glutamate receptor subunits interact with specific PDZ domain-containing proteins. NMDA receptor NR2 subunits bind to the PSD-95 family of proteins, whereas AMPA receptor subunits GluR2/3 bind to GRIP. These interactions may underlie the clustering, targeting, and immobilization of the glutamate receptors at postsynaptic sites. By virtue of their multiple protein-binding domains (e.g., three PDZs in PSD-95 and seven PDZs in GRIP), PSD-95 and GRIP can function as multivalent proteins that organize a specific cytoskeletal and signaling complex associated with each class of glutamate receptor. The network of protein-protein interactions mediated by these abundant PDZ proteins is likely to contribute significantly to the molecular scaffold of the postsynaptic density.[1]References
- Glutamate receptor anchoring proteins and the molecular organization of excitatory synapses. Sheng, M., Pak, D.T. Ann. N. Y. Acad. Sci. (1999) [Pubmed]
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