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Alpha subunit-dependent glycine receptor clustering and regulation of synaptic receptor numbers
Accumulation of glycine receptors at synapses requires the interaction between the beta subunit of the receptor and the scaffold protein gephyrin. Here, we questioned whether different alpha subunits could modulate the receptors’ diffusion and propensity to cluster at spinal cord synapses. Using qua...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5589798/ https://www.ncbi.nlm.nih.gov/pubmed/28883437 http://dx.doi.org/10.1038/s41598-017-11264-3 |
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author | Patrizio, A. Renner, M. Pizzarelli, R. Triller, A. Specht, C. G. |
author_facet | Patrizio, A. Renner, M. Pizzarelli, R. Triller, A. Specht, C. G. |
author_sort | Patrizio, A. |
collection | PubMed |
description | Accumulation of glycine receptors at synapses requires the interaction between the beta subunit of the receptor and the scaffold protein gephyrin. Here, we questioned whether different alpha subunits could modulate the receptors’ diffusion and propensity to cluster at spinal cord synapses. Using quantitative photoactivated localisation microscopy we found that alpha-1 and alpha-3 containing glycine receptors display the same α(3):β(2) stoichiometry and gephyrin binding. Despite these similarities, alpha-3 containing receptors are less mobile and cluster at higher density compared to alpha-1, with 1500 versus 1100 complexes µm(−2), respectively. Furthermore, we identified a subunit-specific regulation of glycine receptor copy numbers at synapses: when challenged with interleukin 1β, the synaptic occupancy of alpha-1 but not alpha-3 receptors was reduced. This mechanism may play a role in the cell-type dependent regulation of glycinergic currents in response to interleukin 1β and highlights the capacity of the alpha subunits to affect receptor-gephyrin binding at synapses. |
format | Online Article Text |
id | pubmed-5589798 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-55897982017-09-13 Alpha subunit-dependent glycine receptor clustering and regulation of synaptic receptor numbers Patrizio, A. Renner, M. Pizzarelli, R. Triller, A. Specht, C. G. Sci Rep Article Accumulation of glycine receptors at synapses requires the interaction between the beta subunit of the receptor and the scaffold protein gephyrin. Here, we questioned whether different alpha subunits could modulate the receptors’ diffusion and propensity to cluster at spinal cord synapses. Using quantitative photoactivated localisation microscopy we found that alpha-1 and alpha-3 containing glycine receptors display the same α(3):β(2) stoichiometry and gephyrin binding. Despite these similarities, alpha-3 containing receptors are less mobile and cluster at higher density compared to alpha-1, with 1500 versus 1100 complexes µm(−2), respectively. Furthermore, we identified a subunit-specific regulation of glycine receptor copy numbers at synapses: when challenged with interleukin 1β, the synaptic occupancy of alpha-1 but not alpha-3 receptors was reduced. This mechanism may play a role in the cell-type dependent regulation of glycinergic currents in response to interleukin 1β and highlights the capacity of the alpha subunits to affect receptor-gephyrin binding at synapses. Nature Publishing Group UK 2017-09-07 /pmc/articles/PMC5589798/ /pubmed/28883437 http://dx.doi.org/10.1038/s41598-017-11264-3 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Patrizio, A. Renner, M. Pizzarelli, R. Triller, A. Specht, C. G. Alpha subunit-dependent glycine receptor clustering and regulation of synaptic receptor numbers |
title | Alpha subunit-dependent glycine receptor clustering and regulation of synaptic receptor numbers |
title_full | Alpha subunit-dependent glycine receptor clustering and regulation of synaptic receptor numbers |
title_fullStr | Alpha subunit-dependent glycine receptor clustering and regulation of synaptic receptor numbers |
title_full_unstemmed | Alpha subunit-dependent glycine receptor clustering and regulation of synaptic receptor numbers |
title_short | Alpha subunit-dependent glycine receptor clustering and regulation of synaptic receptor numbers |
title_sort | alpha subunit-dependent glycine receptor clustering and regulation of synaptic receptor numbers |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5589798/ https://www.ncbi.nlm.nih.gov/pubmed/28883437 http://dx.doi.org/10.1038/s41598-017-11264-3 |
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