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The Journal of Neuroscience, July 1, 2002, 22(13):5387-5392
Critical Postsynaptic Density 95/Disc Large/Zonula
Occludens-1 Interactions by Glutamate Receptor 1 (GluR1)
and GluR2 Required at Different Subcellular Sites
Antonella
Piccini and
Roberto
Malinow
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724
Interactions between AMPA receptor subunits and proteins containing
postsynaptic density 95/disc large/zonula occludens-1 (PDZ)
domains have been shown to play critical roles in the proper trafficking of receptors to excitatory synapses. Synaptic accumulation of AMPA receptors containing the glutamate receptor 1 (GluR1) subunit can be driven by calcium/calmodulin-dependent protein kinase II
activity or long-term potentiation and requires an interaction between
GluR1 and a type I PDZ domain-containing protein. Synaptic incorporation of AMPA receptors with only GluR2 occurs continuously, and this requires an interaction between GluR2 and a type II PDZ domain-containing protein. We used dual-channel, two-photon laser scanning microscopy to provide high-resolution visualization and quantification of green fluorescent protein-tagged AMPA receptors in
different subcellular compartments. We showed that mutations on GluR1
or GluR2 AMPA subunit that perturb interactions with PDZ domain
proteins lead to the accumulation of these receptors at different
subcellular sites. GluR1 mutants accumulate in the dendrite, whereas
GluR2 mutants accumulate in dendritic spines. This suggests that the
critical PDZ domain interactions are required for entry into spines for
GluR1 and for entry into synapses for GluR2.
Key words:
GluR1; GluR2; PDZ domain protein; two-photon laser
scanning imaging; dendrite; dendritic spine; organotypic slice
culture
Copyright © 2002 Society for Neuroscience 0270-6474/02/22135387-06$05.00/0
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