ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2011
Endocytosis of the glutamate receptor subunit GluK3 controls polarized trafficking.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Structure, Function, and Regulation of the Kainate Receptor.Sub-cellular biochemistry · 2022Review
- Significance of transcytosis in Alzheimer's disease: BACE1 takes the scenic route to axons.BioEssays : news and reviews in molecular, cellular and developmental biology · 2015Article
- Trafficking of kainate receptors.Membranes · 2014Review
- Axonal BACE1 dynamics and targeting in hippocampal neurons: a role for Rab11 GTPase.Molecular neurodegeneration · 2014Article
- Agonist-dependent endocytosis of γ-aminobutyric acid type A (GABAA) receptors revealed by a γ2(R43Q) epilepsy mutation.The Journal of biological chemistry · 2013Article
- Kainate receptor post-translational modifications differentially regulate association with 4.1N to control activity-dependent receptor endocytosis.The Journal of biological chemistry · 2013Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kainate receptors (KARs) are widely expressed in the brain and are present at both presynaptic and postsynaptic sites. GluK3-containing KARs are thought to compose presynaptic autoreceptors that facilitate hippocampal mossy fiber synaptic transmission. Here we identify molecular mechanisms that underlie the polarized trafficking of KARs composed of the GluK3b splice variant. Endocytosis followed by degradation is driven by a dileucine motif on the cytoplasmic C-terminal domain of GluK3b in heterologous cells, in cultured hippocampal neurons, and in dentate granule cells from organotypic slice cultures. The internalization of GluK3b is clathrin and dynamin2 dependent. GluK3b is differentially endocytosed in dendrites as compared to the axons. These data suggest that the polarized trafficking of KARs in neurons could be controlled by the regulation of receptor endocytosis.
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Registered trials
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