Extracellular Zinc Ion Inhibits ClC-0 Chloride Channels by Facilitating Slow Gating

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Extracellular Zinc Ion Inhibits ClC-0 Chloride Channels by Facilitating Slow Gating

Extracellular Zn2+ was found to reversibly inhibit the ClC-0 Cl- channel. The apparent on and off rates of the inhibition were highly temperature sensitive, suggesting an effect of Zn2+ on the slow gating (or inactivation) of ClC-0. In the absence of Zn2+, the rate of the slow-gating relaxation increased with temperature, with a Q10 of approximately 37. Extracellular Zn2+ facilitated the slow-g...

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Temperature Dependence of Fast and Slow Gating Relaxations of ClC-0 Chloride Channels

The chloride channel from the Torpedo electric organ, ClC-0, is the best studied member of a large gene-family (Jentsch, T.J. 1996. Curr. Opin. Neurobiol. 6:303-310.). We investigate the temperature dependence of both the voltage- and chloride-dependent fast gate and of the slow gate of the "double-barreled" ClC-0 expressed in Xenopus oocytes. Kinetics of the fast gate exhibit only a moderate t...

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Elimination of the Slow Gating of Clc-0 Chloride Channel by a Point Mutation

The inactivation of the ClC-0 chloride channel is very temperature sensitive and is greatly facilitated by the binding of a zinc ion (Zn2+) from the extracellular side, leading to a Zn2+-induced current inhibition. To further explore the relation of Zn2+ inhibition and the ClC-0 inactivation, we mutated all 12 cysteine amino acids in the channel and assayed the effect of Zn2+ on these mutants. ...

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Electrostatic Control and Chloride Regulation of the Fast Gating of ClC-0 Chloride Channels

The opening and closing of chloride (Cl-) channels in the ClC family are thought to tightly couple to ion permeation through the channel pore. In the prototype channel of the family, the ClC-0 channel from the Torpedo electric organ, the opening-closing of the pore in the millisecond time range known as "fast gating" is regulated by both external and internal Cl- ions. Although the external Cl-...

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Comment on ion transit pathways and gating in ClC chloride channels.

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ژورنال

عنوان ژورنال: Journal of General Physiology

سال: 1998

ISSN: 0022-1295,1540-7748

DOI: 10.1085/jgp.112.6.715