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

Cristina Arrigoni, Indra Schroeder, Giulia Romani, Van Etten, Gerhard Thiel, Anna Moroni

Research output: Contribution to journalArticlepeer-review

37 Scopus citations

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 KvSynth1, a functional voltage-gated, outwardly rectifying K+ channel. KvSynth1 displays the summed features of its individual components: pore properties of Kcv (selectivity and filter gating) and voltage dependence of Ci-VSP (V1/2 = +56 mV; z of 1), including the depolarizationinduced 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

Original languageEnglish (US)
Pages (from-to)389-395
Number of pages7
JournalJournal of General Physiology
Volume141
Issue number3
DOIs
StatePublished - Mar 2013

ASJC Scopus subject areas

  • Physiology

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