Glutamate receptor anchoring proteins and the molecular organization of excitatory synapses

Ann N Y Acad Sci. 1999 Apr 30;868:483-93. doi: 10.1111/j.1749-6632.1999.tb11317.x.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / chemistry
  • Cytoskeleton / chemistry
  • Drosophila
  • Drosophila Proteins*
  • Membrane Proteins
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism
  • Protein Binding
  • Receptors, AMPA / metabolism
  • Receptors, Glutamate / chemistry*
  • Receptors, N-Methyl-D-Aspartate / metabolism
  • Signal Transduction
  • Synapses / metabolism*

Substances

  • Carrier Proteins
  • Drosophila Proteins
  • Grip protein, Drosophila
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Receptors, AMPA
  • Receptors, Glutamate
  • Receptors, N-Methyl-D-Aspartate
  • postsynaptic density proteins