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Am J Physiol Cell Physiol 281: C231-C240, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 1, C231-C240, July 2001

Regions in the carboxy terminus of alpha -bENaC involved in gating and functional effects of actin

Susan J. Copeland, Bakhrom K. Berdiev, Hong-Long Ji, Jason Lockhart, Suzanne Parker, Catherine M. Fuller, and Dale J. Benos

Department of Physiology and Biophysics, University of Alabama at Birmingham, Birmingham, Alabama 35294

Gating differences occur between the alpha -subunits of the bovine and rat clones of an amiloride-sensitive epithelial Na+ channel (ENaC). Deletion of the carboxy terminus of bovine alpha -ENaC (alpha -bENaC) at R567 converted the gating properties to that of rat alpha -ENaC (alpha -rENaC). The equivalent truncation in alpha -rENaC was without effect on the gating of the rat homologue. The addition of actin to ENaC channels composed of either alpha -rENaC or alpha -bENaC alone produced a twofold reduction in conductance and an increase in open probability. Neither alpha -rENaC (R613X) nor alpha -bENaC (R567X) was responsive to actin. Using a chimera consisting of alpha -rENaC1-615 and alpha -bENaC570-650, we examined several different carboxy-terminal truncation mutants plus and minus actin. When incorporated into planar bilayers, the gating pattern of this construct was identical to wild-type (wt) alpha -bENaC. Premature stop mutations proximal to E685X produced channels with gating patterns like alpha -rENaC. Actin had no effect on the E631X truncation, whereas more distal truncations all interacted with actin, as did wt alpha -bENaC. Key findings were confirmed using channels expressed in Xenopus oocytes and studied by cell-attached patch-clamp recording. Our results suggest that the site of actin regulation at the carboxy terminus of the chimera is located between residues 631 and 644.

alpha -subunit of bovine epithelial sodium channel; planar lipid bilayers; patch clamp; amiloride; ion channels; oocytes


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