Anno2013
AutoriCristina Arrigoni, Indra Schroeder, Giulia Romani, James L. Van Etten, Gerhard Thiel, and Anna Moroni
AbstractThe 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 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.
RivistaThe Journal Of General Physiology
ISSN1540-7748
Impact factor
Volume141
Pagina inizio389
Pagina fine395
Autori IBFGiulia Angelica Maria ROMANI, Anna MORONI
Linee di Ricerca IBFMD.P01.005.001
Sedi IBFIBF.MI