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Proc Natl Acad Sci U S A. 2008 Jan 22;105(3):1032-7. doi: 10.1073/pnas.0711313105. Epub 2008 Jan 14.

Synaptic AMPA receptor subunit trafficking is independent of the C terminus in the GluR2-lacking mouse.

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1
Department of Cellular and Molecular Pharmacology and Physiology, University of California, San Francisco, CA 94143, USA.

Abstract

Glutamate is the primary excitatory neurotransmitter in the brain, and alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) type glutamate receptors mediate most fast synaptic transmission. AMPA receptors are tetrameric assemblies composed from four possible subunits (GluR1-4). In hippocampal pyramidal cells, AMPA receptors are heteromeric receptors containing the GluR2 subunit and either GluR1 or GluR3. It is generally accepted that the trafficking of GluR1/GluR2 receptors to synapses requires activity, whereas GluR2/GluR3 receptors traffic constitutively. It has been suggested that the trafficking is governed by the cytoplasmic C termini of the subunits. Because the basis for this theory relied on the introduction of unnatural, homomeric, calcium-permeable AMPA receptors, we have used the GluR2(-/-) knock out mouse to determine whether the expression of mutated forms of GluR2 can rescue WT synaptic responses. We find that GluR2, lacking its entire C terminus, or a GluR2 chimera containing the C terminus of GluR1, is capable of trafficking to the synapse in the absence of activity. These findings suggest that the GluR2 C terminus is not required for GluR2 synaptic insertion.

PMID:
18195349
PMCID:
PMC2242677
DOI:
10.1073/pnas.0711313105
[Indexed for MEDLINE]
Free PMC Article
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