Premium
Glutamate Receptor Anchoring Proteins and the Molecular Organization of Excitatory Synapses
Author(s) -
SHENG MORGAN,
PAK DANIEL T.
Publication year - 1999
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1999.tb11317.x
Subject(s) - postsynaptic density , pdz domain , ampa receptor , glutamate receptor , postsynaptic potential , excitatory postsynaptic potential , microbiology and biotechnology , silent synapse , scaffold protein , ionotropic glutamate receptor , receptor , chemistry , nmda receptor , biology , biochemistry , signal transduction
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.