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¹ Department of Cellular and Physiological Sciences, University of British Columbia, 2146 Health Sciences Mall, Vancouver B.C. V6T 1Z3, Canada

P/C-type inactivation of Kv channels is thought to involve conformational changes in the outer pore of the channel, culminating in a partial constriction of the selectivity filter. Recent studies have identified a number of phenotypic differences in the inactivation properties of different Kv channels, including different sensitivities to elevation of extracellular K⁺ concentration, and different state dependencies of inactivation. We have demonstrated that an alternatively spliced short form of Kv1.5, resulting in disruption of the T1 domain, exhibits a shift in the state dependence of inactivation in this channel, and in the current study we have examined this further to contrast the properties of inactivation from open versus closed states. In a TEA⁺-sensitive mutant of Kv1.5 (Kv1.5 R487T), 10 mM extracellular TEA⁺ inhibits inactivation in both full-length and T1-deleted channels, but does not inhibit closed-state inactivation in T1-deleted channel forms. Similarly, substitution of K⁺ and Na⁺ with Cs⁺ ions in the recording medium inhibits inactivation of both full-length and T1-deleted channel forms, but fails to inhibit closed-state inactivation of T1-deleted channels. Collectively, these data distinguish between open-state and closed-state inactivation, and suggest the presence of multiple possible mechanisms of inactivation coexisting in Kv1 channels.

(Received 28 March 2005; accepted after revision 14 July 2005; first published online 14 July 2005)
Corresponding author D. Fedida: 2146 Health Sciences Mall, Vancouver B.C. V6T 1Z3, Canada. Email: fedida{at}interchange.ubc.ca

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