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The Journal of Neuroscience, January 21, 2004, 24(3):679-691; doi:10.1523/JNEUROSCI.4985-03.2004

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Cellular/Molecular
A C-Terminal Determinant of GluR6 Kainate Receptor Trafficking

Sheng Yan,¹ James M. Sanders,¹ Jian Xu,² Yongling Zhu,² Anis Contractor,² and Geoffrey T. Swanson¹

¹Department of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, Texas 77555, and ²Molecular Neurobiology Laboratory, The Salk Institute, La Jolla, California 92037

Intracellular trafficking of ionotropic glutamate receptors is regulated predominantly by determinants in the cytoplasmic C-terminal domain of the subunit proteins. Although AMPA receptors are found at the vast majority of excitatory synapses, synaptic kainate receptors exhibit a much more restricted distribution, suggesting that specific mechanisms exist for selective trafficking of these receptor proteins. In this report, we define a critical forward trafficking motif that is necessary for surface expression of the glutamate receptor 6 (GluR6) kainate receptor as well as chimeric proteins containing only the GluR6 C-terminal domain. The trafficking determinant was identified by tracking surface expression of green fluorescent protein-tagged GluR6 receptors with confocal immunofluorescence in COS-7 cells and cultured neurons and patch-clamp electrophysiology in human embryonic kidney 293 cells. Serial truncation and alanine site mutagenesis of the GluR6 subunit C terminus localized the critical motif to a seven amino acid stretch of predominantly basic residues. Alanine mutation of the trafficking motif reduced kainate receptor current amplitudes by >90% and resulted in retention of the mutated receptors in the endoplasmic reticulum. This forward trafficking domain is the first such identified for kainate receptors.

Key words: glutamate receptor; kainate receptor; trafficking; endoplasmic reticulum; patch clamp; immunofluorescence

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Received June 19, 2003; revised November 14, 2003; accepted November 14, 2003.

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