Molecular mechanisms of glutamate receptor clustering at excitatory synapses

https://doi.org/10.1016/S0959-4388(98)80062-7Get rights and content
Under a Creative Commons license
open archive

Abstract

The targeting of AMPA- and NMDA-type glutamate receptors to synapses in the central nervous system is essential for efficient excitatory synaptic transmission. Recent studies have indicated that protein—protein interactions of these receptors with synaptic proteins that contain PDZ domains are crucial for receptor targeting. NMDA receptors have been found to bind to the PSD-95 family of proteins, whereas AMPA receptors interact with the PDZ-domain-containing protein GRIP (glutamate receptor interacting protein). PSD-95 and GRIP contain multiple PDZ domains as well as other protein—protein interactions motifs that help to form large macromolecular complexes that may be important for the formation and plasticity of synapses.

AMPA
α-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid
DLG
discs large
FasII
fasciclin II
GK
guanylate kinase
GKAP
GK-associated protein
GluR
AMPA-type glutamate receptor
GRIP
glutamate receptor interacting protein
NMDA
N-methyl-d-aspartate
nNOS
neuronal nitric oxide synthase
NR
NMDA receptor
NSF
N-ethylmaleimide-sensitive factor
PDZ
protein interaction motif first found in PSD-95, DLG, Z0-1
PSD-95
postsynaptic density protein of 95 kDa
SAPAP
SAP90/PSD-95-associated protein
SH3
Src homology 3
ZO-1
zona occludens 1

Cited by (0)