The Journal of General Physiology
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Published online September 10, 2007
doi:10.1085/jgp.200709760
The Journal of General Physiology, Vol. 130, No. 4, 351-363
The Rockefeller University Press, 0022-1295 $30.00
© 2007 Engh et al.
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ARTICLE

 The Role of a Conserved Lysine in Chloride- and Voltage-dependent ClC-0 Fast Gating



Anita M. Engh1, José D. Faraldo-Gómez2, and Merritt Maduke1

1 Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305
2 Gordon Center for Integrative Science, University of Chicago, Chicago, IL 60637

Correspondence to Merritt Maduke: maduke{at}stanford.edu

ClC-0 is a chloride channel whose gating is sensitive to voltage, chloride, and pH. In a previous publication, we showed that the K149C mutation causes a +70-mV shift in the voltage dependence of ClC-0 fast gating. In this paper we analyze the effects of a series of mutations at K149 on the voltage and chloride dependence of gating. By fitting our data to the previously proposed four-state model for ClC-0 fast gating, we show which steps in fast-gate opening are likely to be affected by these mutations. Computational analysis of mutant ClC-0 homology models show electrostatic contributions to chloride binding that may partially account for the effects of K149 on gating. The analysis of gating kinetics in combination with the available structural information suggests some of the structural changes likely to underpin fast-gate opening.


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