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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...

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Autores principales: Oishi, Koichiro, Nagamori, Mayu, Kashino, Yasuhiro, Sekiguchi, Hiroshi, Sasaki, Yuji C., Miyazawa, Atsuo, Nishino, Yuri
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
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).
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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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