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Am J Physiol Renal Physiol 286: F1100-F1106, 2004. First published March 2, 2004; doi:10.1152/ajprenal.00344.2003
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ENaC subunit-subunit interactions and inhibition by syntaxin 1A

Bakhrom K. Berdiev,1 Biljana Jovov,1 Ward C. Tucker,2 Anjaparavanda P. Naren,3 Catherine M. Fuller,1 Edwin R. Chapman,2 and Dale J. Benos1

1Department of Physiology and Biophysics, University of Alabama at Birmingham, Birmingham, Alabama 35294; 2Department of Physiology, University of Wisconsin, Madison, Wisconsin 53706; and 3Department of Physiology, University of Tennessee Health Science Center, Memphis, Tennessee 38163

Submitted 26 September 2003 ; accepted in final form 20 January 2004

Amiloride-sensitive epithelial Na+ channels (ENaCs) are subject to modulation by many factors. Recent data have also linked the N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) machinery to this regulation of ENaC, but the molecular mechanisms that underlie this modulation are poorly understood. In this study, we demonstrate that syntaxin 1A physically interacts with ENaC and functionally regulates ENaC activity. Syntaxin 1A was able to coimmunoprecipitate in vitro-translated {gamma}-ENaC, but not {alpha}- or {beta}-ENaC. Also, using antibodies raised against {alpha}-, {beta}-, or {gamma}-ENaC, we detected syntaxin 1A in immunoprecipitates from Madin-Darby canine kidney cells stably transfected with {alpha}{beta}{gamma}-ENaC. In bilayers, syntaxin 1A inhibited ENaC, and this syntaxin 1A modulation of ENaC activity was eliminated by truncations of cytoplasmic domains of the ENaC subunits. Our findings provide evidence for a direct physical interaction between ENaC and syntaxin 1A and suggest involvement of ENaC's cytoplasmic domains in functional modulation of ENaC activity by syntaxin 1A.

membrane; channels; bilayers; interaction


Address for reprint requests and other correspondence: D. J. Benos, Univ. of Alabama at Birmingham, 1918 University Blvd., MCLM 704, Birmingham, AL 35294-0005 (E-mail: benos{at}physiology.uab.edu).




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