Neto auxiliary proteins control both the trafficking and biophysical properties of the kainate receptor GluK1
Kainate receptors (KARs) are a subfamily of glutamate receptors mediating excitatory synaptic transmission and Neto proteins are recently identified auxiliary subunits for KARs. However, the roles of Neto proteins in the synaptic trafficking of KAR GluK1 are poorly understood. Here, using the hippoc...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2015-12-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/11682 |
| _version_ | 1828107643945746432 |
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| author | Nengyin Sheng Yun S Shi Richa Madan Lomash Katherine W Roche Roger A Nicoll |
| author_facet | Nengyin Sheng Yun S Shi Richa Madan Lomash Katherine W Roche Roger A Nicoll |
| author_sort | Nengyin Sheng |
| collection | DOAJ |
| description | Kainate receptors (KARs) are a subfamily of glutamate receptors mediating excitatory synaptic transmission and Neto proteins are recently identified auxiliary subunits for KARs. However, the roles of Neto proteins in the synaptic trafficking of KAR GluK1 are poorly understood. Here, using the hippocampal CA1 pyramidal neuron as a null background system we find that surface expression of GluK1 receptor itself is very limited and is not targeted to excitatory synapses. Both Neto1 and Neto2 profoundly increase GluK1 surface expression and also drive GluK1 to synapses. However, the regulation GluK1 synaptic targeting by Neto proteins is independent of their role in promoting surface trafficking. Interestingly, GluK1 is excluded from synapses expressing AMPA receptors and is selectively incorporated into silent synapses. Neto2, but not Neto1, slows GluK1 deactivation, whereas Neto1 speeds GluK1 desensitization and Neto2 slows desensitization. These results establish critical roles for Neto auxiliary subunits controlling KARs properties and synaptic incorporation. |
| first_indexed | 2024-04-11T10:34:21Z |
| format | Article |
| id | doaj.art-2c34d07d55514bb083c68e838e78a76c |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-11T10:34:21Z |
| publishDate | 2015-12-01 |
| publisher | eLife Sciences Publications Ltd |
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| series | eLife |
| spelling | doaj.art-2c34d07d55514bb083c68e838e78a76c2022-12-22T04:29:20ZengeLife Sciences Publications LtdeLife2050-084X2015-12-01410.7554/eLife.11682Neto auxiliary proteins control both the trafficking and biophysical properties of the kainate receptor GluK1Nengyin Sheng0https://orcid.org/0000-0003-3086-3950Yun S Shi1Richa Madan Lomash2Katherine W Roche3Roger A Nicoll4Deparment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United StatesDeparment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States; The Model Animal Research Center, Key Laboratory of Model Animal for Disease Study of Ministry of Education, Nanjing University, Nanjing, ChinaReceptor Biology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, United StatesReceptor Biology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, United StatesDeparment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, United States; Department of Physiology, University of California, San Francisco, San Francisco, United StatesKainate receptors (KARs) are a subfamily of glutamate receptors mediating excitatory synaptic transmission and Neto proteins are recently identified auxiliary subunits for KARs. However, the roles of Neto proteins in the synaptic trafficking of KAR GluK1 are poorly understood. Here, using the hippocampal CA1 pyramidal neuron as a null background system we find that surface expression of GluK1 receptor itself is very limited and is not targeted to excitatory synapses. Both Neto1 and Neto2 profoundly increase GluK1 surface expression and also drive GluK1 to synapses. However, the regulation GluK1 synaptic targeting by Neto proteins is independent of their role in promoting surface trafficking. Interestingly, GluK1 is excluded from synapses expressing AMPA receptors and is selectively incorporated into silent synapses. Neto2, but not Neto1, slows GluK1 deactivation, whereas Neto1 speeds GluK1 desensitization and Neto2 slows desensitization. These results establish critical roles for Neto auxiliary subunits controlling KARs properties and synaptic incorporation.https://elifesciences.org/articles/11682kainate receptorNetosynaptic traffickingGluK1silent synapse |
| spellingShingle | Nengyin Sheng Yun S Shi Richa Madan Lomash Katherine W Roche Roger A Nicoll Neto auxiliary proteins control both the trafficking and biophysical properties of the kainate receptor GluK1 eLife kainate receptor Neto synaptic trafficking GluK1 silent synapse |
| title | Neto auxiliary proteins control both the trafficking and biophysical properties of the kainate receptor GluK1 |
| title_full | Neto auxiliary proteins control both the trafficking and biophysical properties of the kainate receptor GluK1 |
| title_fullStr | Neto auxiliary proteins control both the trafficking and biophysical properties of the kainate receptor GluK1 |
| title_full_unstemmed | Neto auxiliary proteins control both the trafficking and biophysical properties of the kainate receptor GluK1 |
| title_short | Neto auxiliary proteins control both the trafficking and biophysical properties of the kainate receptor GluK1 |
| title_sort | neto auxiliary proteins control both the trafficking and biophysical properties of the kainate receptor gluk1 |
| topic | kainate receptor Neto synaptic trafficking GluK1 silent synapse |
| url | https://elifesciences.org/articles/11682 |
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