Functional diversity of potassium channel voltage-sensing domains

Channels
León D Islas

Abstract

Voltage-gated potassium channels or Kv's are membrane proteins with fundamental physiological roles. They are composed of 2 main functional protein domains, the pore domain, which regulates ion permeation, and the voltage-sensing domain, which is in charge of sensing voltage and undergoing a conformational change that is later transduced into pore opening. The voltage-sensing domain or VSD is a highly conserved structural motif found in all voltage-gated ion channels and can also exist as an independent feature, giving rise to voltage sensitive enzymes and also sustaining proton fluxes in proton-permeable channels. In spite of the structural conservation of VSDs in potassium channels, there are several differences in the details of VSD function found across variants of Kvs. These differences are mainly reflected in variations in the electrostatic energy needed to open different potassium channels. In turn, the differences in detailed VSD functioning among voltage-gated potassium channels might have physiological consequences that have not been explored and which might reflect evolutionary adaptations to the different roles played by Kv channels in cell physiology.

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Citations

Jan 9, 2017·Biochimica Et Biophysica Acta. Biomembranes·Agata Wawrzkiewicz-JałowieckaZbigniew J Grzywna
Dec 12, 2018·The Journal of General Physiology·Yu Patrick ShiTom W Claydon
Dec 17, 2020·Frontiers in Pharmacology·Carlos A Villalba-Galea, Alvin T Chiem
Feb 3, 2021·Biochimica Et Biophysica Acta. Biomembranes·Anindita Das, H Raghuraman

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Methods Mentioned

BETA
X-ray
x-ray crystallography
LRET

Software Mentioned

TEVC

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