Extracellular K+ and Ba2+ mediate voltage-dependent inactivation of the outward-rectifying K+ channel encoded by the yeast gene TOK1

Vergani, Paola and Miosga, Thomas and Jarvis, Simon M. and Blatt, Michael R. (1997) Extracellular K+ and Ba2+ mediate voltage-dependent inactivation of the outward-rectifying K+ channel encoded by the yeast gene TOK1. FEBS Letters, 405 (3). pp. 337-344. ISSN 0014-5793. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/10.1016/S0014-5793(97)00211-1

Abstract

Gating of the yeast K+ channel encoded by the Saccharomyces cerevisiae gene TOK1, unlike other outward-rectifying K+ channels that have been cloned, is promoted by membrane voltage (inside positive-going) and repressed by extracellular K+. When expressed in Xenopus laevis oocytes, the TOK1p current rectified strongly outward, its activation shifting in parallel with the K+ equilibrium potential when the external K+ concentration ([K+](0)) was increased above 3 mM. Analysis of the TOK1p current indicated that two kinetic components contributed to the conductance and the voltage sensitivity of the conductance. By contrast, the [K+](0) sensitivity of the current was accommodated entirely within the slow-relaxing component; it was diminished near 1 mM [K+](0), and at submillimolar concentrations the voltage dependence of the TOK1p conductance was insensitive to [K+](0). External Rb+, the K+ channel blockers Cs+ and Ba2+ - but not Na+, Ca2+ or Mg2+ - substituted for K+ in control of TOK1p activation, indicating a specificity in cation interaction with the TOK1p gate. These and additional results indicate that external K+ acts as a ligand to inactivate the TOK1p channel, and they implicate a gating process mediated by a single cation binding site within the membrane electric field, but distinct from the permeation pathway. (C) 1997 Federation of European Biochemical Societies.

Item Type: Article
Subjects: Q Science > QR Microbiology
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: T.J. Sango
Date Deposited: 05 May 2009 07:37
Last Modified: 24 Apr 2014 07:58
Resource URI: https://kar.kent.ac.uk/id/eprint/18006 (The current URI for this page, for reference purposes)
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