The Journal of General Physiology
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Published 30 October 2000. doi:10.1085/jgp.116.5.721
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© The Rockefeller University Press, 0022-1295/2000/11/721/ $5.00
The Journal of General Physiology, Volume 116, Number 5, November 1, 2000 721-734

Original Article

Opening and Closing of KCNKØ Potassium Leak Channels Is Tightly Regulated

Noam Zilberberga,b, Nitza Ilana,b, Rosana Gonzalez-Colasoa,b, and Steve A.N. Goldsteina,b
a Department of Pediatrics, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, Connecticut 06536
b Department of Cellular and Molecular Physiology, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, Connecticut 06536

Correspondence to: Steve A.N. Goldstein, Section of Developmental Biology and Biophysics, 295 Congress Avenue, New Haven, CT 06536. Fax:(203) 737-2290 E-mail:steve.goldstein{at}yale.edu.

Potassium-selective leak channels control neuromuscular function through effects on membrane excitability. Nonetheless, their existence as independent molecular entities was established only recently with the cloning of KCNKØ from Drosophila melanogaster. Here, the operating mechanism of these 2 P domain leak channels is delineated. Single KCNKØ channels switch between two long-lived states (one open and one closed) in a tenaciously regulated fashion. Activation can increase the open probability to ~1, and inhibition can reduce it to ~0.05. Gating is dictated by a 700-residue carboxy-terminal tail that controls the closed state dwell time but does not form a channel gate; its deletion (to produce a 300-residue subunit with two P domains and four transmembrane segments) yields unregulated leak channels that enter, but do not maintain, the closed state. The tail integrates simultaneous input from multiple regulatory pathways acting via protein kinases C, A, and G.

Key Words: background conductance, 2 P domain, protein kinases C, A, and G, open rectifier , ORK1


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