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Ligand-Dependent Intramolecular Motion of Native Nicotinic Acetylcholine Receptors Determined in Living Myotube Cells via Diffracted X-ray Tracking
Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels that play an important role in signal transduction at the neuromuscular junction (NMJ). Movement of the nAChR extracellular domain following agonist binding induces conformational changes in the extracellular domain, which in t...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10418694/ https://www.ncbi.nlm.nih.gov/pubmed/37569445 http://dx.doi.org/10.3390/ijms241512069 |
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author | Oishi, Koichiro Nagamori, Mayu Kashino, Yasuhiro Sekiguchi, Hiroshi Sasaki, Yuji C. Miyazawa, Atsuo Nishino, Yuri |
author_facet | Oishi, Koichiro Nagamori, Mayu Kashino, Yasuhiro Sekiguchi, Hiroshi Sasaki, Yuji C. Miyazawa, Atsuo Nishino, Yuri |
author_sort | Oishi, Koichiro |
collection | PubMed |
description | Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels that play an important role in signal transduction at the neuromuscular junction (NMJ). Movement of the nAChR extracellular domain following agonist binding induces conformational changes in the extracellular domain, which in turn affects the transmembrane domain and opens the ion channel. It is known that the surrounding environment, such as the presence of specific lipids and proteins, affects nAChR function. Diffracted X-ray tracking (DXT) facilitates measurement of the intermolecular motions of receptors on the cell membranes of living cells, including all the components involved in receptor function. In this study, the intramolecular motion of the extracellular domain of native nAChR proteins in living myotube cells was analyzed using DXT for the first time. We revealed that the motion of the extracellular domain in the presence of an agonist (e.g., carbamylcholine, CCh) was restricted by an antagonist (i.e., alpha-bungarotoxin, BGT). |
format | Online Article Text |
id | pubmed-10418694 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-104186942023-08-12 Ligand-Dependent Intramolecular Motion of Native Nicotinic Acetylcholine Receptors Determined in Living Myotube Cells via Diffracted X-ray Tracking Oishi, Koichiro Nagamori, Mayu Kashino, Yasuhiro Sekiguchi, Hiroshi Sasaki, Yuji C. Miyazawa, Atsuo Nishino, Yuri Int J Mol Sci Communication Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels that play an important role in signal transduction at the neuromuscular junction (NMJ). Movement of the nAChR extracellular domain following agonist binding induces conformational changes in the extracellular domain, which in turn affects the transmembrane domain and opens the ion channel. It is known that the surrounding environment, such as the presence of specific lipids and proteins, affects nAChR function. Diffracted X-ray tracking (DXT) facilitates measurement of the intermolecular motions of receptors on the cell membranes of living cells, including all the components involved in receptor function. In this study, the intramolecular motion of the extracellular domain of native nAChR proteins in living myotube cells was analyzed using DXT for the first time. We revealed that the motion of the extracellular domain in the presence of an agonist (e.g., carbamylcholine, CCh) was restricted by an antagonist (i.e., alpha-bungarotoxin, BGT). MDPI 2023-07-28 /pmc/articles/PMC10418694/ /pubmed/37569445 http://dx.doi.org/10.3390/ijms241512069 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Communication Oishi, Koichiro Nagamori, Mayu Kashino, Yasuhiro Sekiguchi, Hiroshi Sasaki, Yuji C. Miyazawa, Atsuo Nishino, Yuri Ligand-Dependent Intramolecular Motion of Native Nicotinic Acetylcholine Receptors Determined in Living Myotube Cells via Diffracted X-ray Tracking |
title | Ligand-Dependent Intramolecular Motion of Native Nicotinic Acetylcholine Receptors Determined in Living Myotube Cells via Diffracted X-ray Tracking |
title_full | Ligand-Dependent Intramolecular Motion of Native Nicotinic Acetylcholine Receptors Determined in Living Myotube Cells via Diffracted X-ray Tracking |
title_fullStr | Ligand-Dependent Intramolecular Motion of Native Nicotinic Acetylcholine Receptors Determined in Living Myotube Cells via Diffracted X-ray Tracking |
title_full_unstemmed | Ligand-Dependent Intramolecular Motion of Native Nicotinic Acetylcholine Receptors Determined in Living Myotube Cells via Diffracted X-ray Tracking |
title_short | Ligand-Dependent Intramolecular Motion of Native Nicotinic Acetylcholine Receptors Determined in Living Myotube Cells via Diffracted X-ray Tracking |
title_sort | ligand-dependent intramolecular motion of native nicotinic acetylcholine receptors determined in living myotube cells via diffracted x-ray tracking |
topic | Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10418694/ https://www.ncbi.nlm.nih.gov/pubmed/37569445 http://dx.doi.org/10.3390/ijms241512069 |
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