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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