Abstract
Kainate receptors mediate glutamatergic signaling through both pre- and presynaptic receptors. Here, we studied the expression of the high affinity kainate receptor GluK5 in the mouse retina. Double-immunofluoresence labeling and electron microscopic analysis revealed a presynaptic localization of GluK5 in the outer plexiform layer. Unexpectedly, we found GluK5 almost exclusively localized to the presynaptic ribbon of photoreceptor terminals. Moreover, in GluK5-deficient mutant mice the structural integrity of synaptic ribbons was severely altered pointing to a novel function of GluK5 in organizing synaptic ribbons in the presynaptic terminals of rod photoreceptors.
MeSH terms
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Alcohol Oxidoreductases
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Animals
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Co-Repressor Proteins
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DNA-Binding Proteins / metabolism
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Mice, 129 Strain
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Mice, Inbred C57BL
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Mice, Knockout
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Organ Specificity
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Phosphoproteins / metabolism
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Presynaptic Terminals / metabolism*
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Protein Transport
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Receptors, Kainic Acid / metabolism*
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Retina / metabolism
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Retina / ultrastructure
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Retinal Rod Photoreceptor Cells / metabolism*
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Retinal Rod Photoreceptor Cells / ultrastructure
Substances
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Co-Repressor Proteins
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DNA-Binding Proteins
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Gluk1 kainate receptor
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Phosphoproteins
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Receptors, Kainic Acid
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Alcohol Oxidoreductases
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Ctbp2 protein, mouse
Grants and funding
This work was supported by the German Research Foundation (FR 620/14-1 to MF); Landesforschungsförderung by the State of Hamburg (LFF-FV27, project P3) to MF. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.