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

Arrigoni, Cristina ; Schroeder, Indra ; Romani, Giulia ; Etten, James L. van ; Thiel, Gerhard ; Moroni, Anna (2013)
The voltage-sensing domain of a phosphatase gates the pore of a potassium channel.
In: The Journal of general physiology, 141 (3)
Artikel, Bibliographie

Kurzbeschreibung (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.

Typ des Eintrags: Artikel
Erschienen: 2013
Autor(en): Arrigoni, Cristina ; Schroeder, Indra ; Romani, Giulia ; Etten, James L. van ; Thiel, Gerhard ; Moroni, Anna
Art des Eintrags: Bibliographie
Titel: The voltage-sensing domain of a phosphatase gates the pore of a potassium channel.
Sprache: Englisch
Publikationsjahr: 2013
Titel der Zeitschrift, Zeitung oder Schriftenreihe: The Journal of general physiology
Jahrgang/Volume einer Zeitschrift: 141
(Heft-)Nummer: 3
Kurzbeschreibung (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.

Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > Plant Membrane Biophyscis (am 20.12.23 umbenannt in Biologie der Algen und Protozoen)
Hinterlegungsdatum: 28 Mär 2013 07:42
Letzte Änderung: 20 Aug 2021 09:43
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