Tracking the movement of discrete gating charges in a voltage-gated potassium channel

Positively charged amino acids respond to membrane potential changes to drive voltage sensor movement in voltage-gated ion channels, but determining the displacements of voltage sensor gating charges has proven difficult. We optically tracked the movement of the two most extracellular charged residu...

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Autores principales:	Michael F Priest, Elizabeth EL Lee, Francisco Bezanilla
Formato:	article
Lenguaje:	EN
Publicado:	eLife Sciences Publications Ltd 2021
Materias:	voltage sensor shaker fluorescence quenching bimane sensor path Medicine R Science Q Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/653d41c01d7942449409f97e536ef6d3
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id	oai:doaj.org-article:653d41c01d7942449409f97e536ef6d3
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spelling	oai:doaj.org-article:653d41c01d7942449409f97e536ef6d32021-12-01T13:54:34ZTracking the movement of discrete gating charges in a voltage-gated potassium channel10.7554/eLife.581482050-084Xe58148https://doaj.org/article/653d41c01d7942449409f97e536ef6d32021-11-01T00:00:00Zhttps://elifesciences.org/articles/58148https://doaj.org/toc/2050-084XPositively charged amino acids respond to membrane potential changes to drive voltage sensor movement in voltage-gated ion channels, but determining the displacements of voltage sensor gating charges has proven difficult. We optically tracked the movement of the two most extracellular charged residues (R1 and R2) in the Shaker potassium channel voltage sensor using a fluorescent positively charged bimane derivative (qBBr) that is strongly quenched by tryptophan. By individually mutating residues to tryptophan within the putative pathway of gating charges, we observed that the charge motion during activation is a rotation and a tilted translation that differs between R1 and R2. Tryptophan-induced quenching of qBBr also indicates that a crucial residue of the hydrophobic plug is linked to the Cole–Moore shift through its interaction with R1. Finally, we show that this approach extends to additional voltage-sensing membrane proteins using the Ciona intestinalis voltage-sensitive phosphatase (CiVSP).Michael F PriestElizabeth EL LeeFrancisco BezanillaeLife Sciences Publications Ltdarticlevoltage sensorshakerfluorescence quenchingbimanesensor pathMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	voltage sensor shaker fluorescence quenching bimane sensor path Medicine R Science Q Biology (General) QH301-705.5
spellingShingle	voltage sensor shaker fluorescence quenching bimane sensor path Medicine R Science Q Biology (General) QH301-705.5 Michael F Priest Elizabeth EL Lee Francisco Bezanilla Tracking the movement of discrete gating charges in a voltage-gated potassium channel
description	Positively charged amino acids respond to membrane potential changes to drive voltage sensor movement in voltage-gated ion channels, but determining the displacements of voltage sensor gating charges has proven difficult. We optically tracked the movement of the two most extracellular charged residues (R1 and R2) in the Shaker potassium channel voltage sensor using a fluorescent positively charged bimane derivative (qBBr) that is strongly quenched by tryptophan. By individually mutating residues to tryptophan within the putative pathway of gating charges, we observed that the charge motion during activation is a rotation and a tilted translation that differs between R1 and R2. Tryptophan-induced quenching of qBBr also indicates that a crucial residue of the hydrophobic plug is linked to the Cole–Moore shift through its interaction with R1. Finally, we show that this approach extends to additional voltage-sensing membrane proteins using the Ciona intestinalis voltage-sensitive phosphatase (CiVSP).
format	article
author	Michael F Priest Elizabeth EL Lee Francisco Bezanilla
author_facet	Michael F Priest Elizabeth EL Lee Francisco Bezanilla
author_sort	Michael F Priest
title	Tracking the movement of discrete gating charges in a voltage-gated potassium channel
title_short	Tracking the movement of discrete gating charges in a voltage-gated potassium channel
title_full	Tracking the movement of discrete gating charges in a voltage-gated potassium channel
title_fullStr	Tracking the movement of discrete gating charges in a voltage-gated potassium channel
title_full_unstemmed	Tracking the movement of discrete gating charges in a voltage-gated potassium channel
title_sort	tracking the movement of discrete gating charges in a voltage-gated potassium channel
publisher	eLife Sciences Publications Ltd
publishDate	2021
url	https://doaj.org/article/653d41c01d7942449409f97e536ef6d3
work_keys_str_mv	AT michaelfpriest trackingthemovementofdiscretegatingchargesinavoltagegatedpotassiumchannel AT elizabethellee trackingthemovementofdiscretegatingchargesinavoltagegatedpotassiumchannel AT franciscobezanilla trackingthemovementofdiscretegatingchargesinavoltagegatedpotassiumchannel
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Tracking the movement of discrete gating charges in a voltage-gated potassium channel

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