The voltage-sensing domain of a phosphatase gates the pore of a potassium channel (Articolo in rivista)

Type
Label
  • The voltage-sensing domain of a phosphatase gates the pore of a potassium channel (Articolo in rivista) (literal)
Anno
  • 2013-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1085/jgp.201210940 (literal)
Alternative label
  • Cristina Arrigoni, Indra Schroeder, Giulia Romani, James L. Van Etten, Gerhard Thiel, and Anna Moroni (2013)
    The voltage-sensing domain of a phosphatase gates the pore of a potassium channel
    in The journal of general physiology (Online)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Cristina Arrigoni, Indra Schroeder, Giulia Romani, James L. Van Etten, Gerhard Thiel, and Anna Moroni (literal)
Pagina inizio
  • 389 (literal)
Pagina fine
  • 395 (literal)
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  • 141 (literal)
Rivista
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  • 7 (literal)
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  • 3 (literal)
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  • Department of Biosciences and 2Institute of Biophysics, Consiglio Nazionale delle Ricerche, Università degli Studi di Milano, 20133 Milano, Italy 3Plant Membrane Biophysics, Technische Universität Darmstadt, 64287 Darmstadt, Germany 4Department of Plant Pathology and 5Nebraska Center for Virology, University of Nebraska, Lincoln, NE 68583 (literal)
Titolo
  • The voltage-sensing domain of a phosphatase gates the pore of a potassium channel (literal)
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 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. (literal)
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