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Cell Rep. 2016 Jul 12;16(2):531-544. doi: 10.1016/j.celrep.2016.05.093. Epub 2016 Jun 23.

Distinct Subunit Domains Govern Synaptic Stability and Specificity of the Kainate Receptor.

Author information

1
Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520.
2
CNNR Program, Department of Neuroscience, Yale University School of Medicine, New Haven, CT 06520.
3
Department of Physiology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
4
Department of Anatomy, Hokkaido University Graduate School of Medicine, Sapporo 060-8638, Japan.
5
Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06520.
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Contributed equally

Abstract

Synaptic communication between neurons requires the precise localization of neurotransmitter receptors to the correct synapse type. Kainate-type glutamate receptors restrict synaptic localization that is determined by the afferent presynaptic connection. The mechanisms that govern this input-specific synaptic localization remain unclear. Here, we examine how subunit composition and specific subunit domains contribute to synaptic localization of kainate receptors. The cytoplasmic domain of the GluK2 low-affinity subunit stabilizes kainate receptors at synapses. In contrast, the extracellular domain of the GluK4/5 high-affinity subunit synergistically controls the synaptic specificity of kainate receptors through interaction with C1q-like proteins. Thus, the input-specific synaptic localization of the native kainate receptor complex involves two mechanisms that underlie specificity and stabilization of the receptor at synapses.

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