The gating mechanism in cyclic nucleotide-gated ion channels

Abstract Cyclic nucleotide-gated (CNG) channels mediate transduction in several sensory neurons. These channels use the free energy of CNs’ binding to open the pore, a process referred to as gating. CNG channels belong to the superfamily of voltage-gated channels, where the motion of the α-helix S6...

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Autores principales:	Monica Mazzolini, Manuel Arcangeletti, Arin Marchesi, Luisa M. R. Napolitano, Debora Grosa, Sourav Maity, Claudio Anselmi, Vincent Torre
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/60a94f99df51492fb6ad132b1af0b964
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spelling	oai:doaj.org-article:60a94f99df51492fb6ad132b1af0b9642021-12-02T15:08:55ZThe gating mechanism in cyclic nucleotide-gated ion channels10.1038/s41598-017-18499-02045-2322https://doaj.org/article/60a94f99df51492fb6ad132b1af0b9642018-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-18499-0https://doaj.org/toc/2045-2322Abstract Cyclic nucleotide-gated (CNG) channels mediate transduction in several sensory neurons. These channels use the free energy of CNs’ binding to open the pore, a process referred to as gating. CNG channels belong to the superfamily of voltage-gated channels, where the motion of the α-helix S6 controls gating in most of its members. To date, only the open, cGMP-bound, structure of a CNG channel has been determined at atomic resolution, which is inadequate to determine the molecular events underlying gating. By using electrophysiology, site-directed mutagenesis, chemical modification, and Single Molecule Force Spectroscopy, we demonstrate that opening of CNGA1 channels is initiated by the formation of salt bridges between residues in the C-linker and S5 helix. These events trigger conformational changes of the α-helix S5, transmitted to the P-helix and leading to channel opening. Therefore, the superfamily of voltage-gated channels shares a similar molecular architecture but has evolved divergent gating mechanisms.Monica MazzoliniManuel ArcangelettiArin MarchesiLuisa M. R. NapolitanoDebora GrosaSourav MaityClaudio AnselmiVincent TorreNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-15 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Monica Mazzolini Manuel Arcangeletti Arin Marchesi Luisa M. R. Napolitano Debora Grosa Sourav Maity Claudio Anselmi Vincent Torre The gating mechanism in cyclic nucleotide-gated ion channels
description	Abstract Cyclic nucleotide-gated (CNG) channels mediate transduction in several sensory neurons. These channels use the free energy of CNs’ binding to open the pore, a process referred to as gating. CNG channels belong to the superfamily of voltage-gated channels, where the motion of the α-helix S6 controls gating in most of its members. To date, only the open, cGMP-bound, structure of a CNG channel has been determined at atomic resolution, which is inadequate to determine the molecular events underlying gating. By using electrophysiology, site-directed mutagenesis, chemical modification, and Single Molecule Force Spectroscopy, we demonstrate that opening of CNGA1 channels is initiated by the formation of salt bridges between residues in the C-linker and S5 helix. These events trigger conformational changes of the α-helix S5, transmitted to the P-helix and leading to channel opening. Therefore, the superfamily of voltage-gated channels shares a similar molecular architecture but has evolved divergent gating mechanisms.
format	article
author	Monica Mazzolini Manuel Arcangeletti Arin Marchesi Luisa M. R. Napolitano Debora Grosa Sourav Maity Claudio Anselmi Vincent Torre
author_facet	Monica Mazzolini Manuel Arcangeletti Arin Marchesi Luisa M. R. Napolitano Debora Grosa Sourav Maity Claudio Anselmi Vincent Torre
author_sort	Monica Mazzolini
title	The gating mechanism in cyclic nucleotide-gated ion channels
title_short	The gating mechanism in cyclic nucleotide-gated ion channels
title_full	The gating mechanism in cyclic nucleotide-gated ion channels
title_fullStr	The gating mechanism in cyclic nucleotide-gated ion channels
title_full_unstemmed	The gating mechanism in cyclic nucleotide-gated ion channels
title_sort	gating mechanism in cyclic nucleotide-gated ion channels
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/60a94f99df51492fb6ad132b1af0b964
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The gating mechanism in cyclic nucleotide-gated ion channels

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