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J. Biol. Chem., Vol. 281, Issue 10, 6528-6538, March 10, 2006

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The Carboxyl Terminus of the -Subunit of the Amiloride-sensitive Epithelial Sodium Channel Binds to F-actin^*

Christopher Mazzochi, James K. Bubien, Peter R. Smith, and Dale J. Benos¹

From the Department of Physiology and Biophysics and Department of Cell Biology, The University of Alabama at Birmingham, Birmingham, Alabama 35294

The activity of the amiloride-sensitive epithelial sodium channel (ENaC) is modulated by F-actin. However, it is unknown if there is a direct interaction between -ENaC and actin. We have investigated the hypothesis that the actin cytoskeleton directly binds to the carboxyl terminus of -ENaC using a combination of confocal microscopy, co-immunoprecipitation, and protein binding studies. Confocal microscopy of Madin-Darby canine kidney cell monolayers stably transfected with wild type, rat isoforms of -, -, and -ENaC revealed co-localization of -ENaC with the cortical F-actin cytoskeleton both at the apical membrane and within the subapical cytoplasm. F-actin was found to co-immunoprecipitate with -ENaC from whole cell lysates of this cell line. Gel overlay assays demonstrated that F-actin specifically binds to the carboxyl terminus of -ENaC. A direct interaction between F-actin and the COOH terminus of -ENaC was further corroborated by F-actin co-sedimentation studies. This is the first study to report a direct and specific biochemical interaction between F-actin and ENaC.

Received for publication, August 25, 2005 , and in revised form, December 14, 2005.

^* This work was supported by National Institutes of Health Grant DK37206. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Physiology and Biophysics, MCLM 704, University of Alabama at Birmingham, 1918 University Blvd., Birmingham, AL 35294-0005. Tel.: 205-934-6220; Fax: 205-934-2377; E-mail: benos{at}physiology.uab.edu.

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