Journal
JOURNAL OF GENERAL PHYSIOLOGY
Volume 141, Issue 3, Pages 389-395Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1085/jgp.201210940
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Funding
- PRIN
- Progetto di Cooperazione Scientifica e Tecnologica Regione Lombardia [SAL-49]
- Cariplo [2009-3519]
- LOEWE initiative Soft Control
- National Science Foundation-EPSCoR [EPS-1004094]
- COBRE program of the National Center for Research Resources [P20-RR15635]
- EPSCoR [1004094] Funding Source: National Science Foundation
- Office Of The Director [1004094] Funding Source: National Science Foundation
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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 similar to 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.
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