TU Darmstadt / ULB / TUbiblio

The voltage-sensing domain of a phosphatase gates the pore of a potassium channel.

Arrigoni, Cristina and Schroeder, Indra and Romani, Giulia and Van Etten, James L. and Thiel, Gerhard and Moroni, Anna (2013):
The voltage-sensing domain of a phosphatase gates the pore of a potassium channel.
In: The Journal of general physiology, pp. 389-95, 141, (3), ISSN 1540-7748,
[Article]

Abstract

The modular architecture of voltage-gated K(+) (Kv) channels suggests that they resulted from the fusion of a voltage-sensing domain (VSD) to a pore module. Here, we show that the VSD of Ciona intestinalis phosphatase (Ci-VSP) fused to the viral channel Kcv creates Kv(Synth1), a functional voltage-gated, outwardly rectifying K(+) channel. Kv(Synth1) displays the summed features of its individual components: pore properties of Kcv (selectivity and filter gating) and voltage dependence of Ci-VSP (V(1/2) = +56 mV; z of ~1), including the depolarization-induced mode shift. The degree of outward rectification of the channel is critically dependent on the length of the linker more than on its amino acid composition. This highlights a mechanistic role of the linker in transmitting the movement of the sensor to the pore and shows that electromechanical coupling can occur without coevolution of the two domains.

Item Type: Article
Erschienen: 2013
Creators: Arrigoni, Cristina and Schroeder, Indra and Romani, Giulia and Van Etten, James L. and Thiel, Gerhard and Moroni, Anna
Title: The voltage-sensing domain of a phosphatase gates the pore of a potassium channel.
Language: English
Abstract:

The modular architecture of voltage-gated K(+) (Kv) channels suggests that they resulted from the fusion of a voltage-sensing domain (VSD) to a pore module. Here, we show that the VSD of Ciona intestinalis phosphatase (Ci-VSP) fused to the viral channel Kcv creates Kv(Synth1), a functional voltage-gated, outwardly rectifying K(+) channel. Kv(Synth1) displays the summed features of its individual components: pore properties of Kcv (selectivity and filter gating) and voltage dependence of Ci-VSP (V(1/2) = +56 mV; z of ~1), including the depolarization-induced mode shift. The degree of outward rectification of the channel is critically dependent on the length of the linker more than on its amino acid composition. This highlights a mechanistic role of the linker in transmitting the movement of the sensor to the pore and shows that electromechanical coupling can occur without coevolution of the two domains.

Journal or Publication Title: The Journal of general physiology
Volume: 141
Number: 3
Divisions: 10 Department of Biology
10 Department of Biology > Plant Membrane Biophysics
Date Deposited: 28 Mar 2013 07:42
Export:
Suche nach Titel in: TUfind oder in Google

Optionen (nur für Redakteure)

View Item View Item