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J. Biol. Chem., Vol. 275, Issue 36, 27947-27956, September 8, 2000
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From the Epithelial sodium channel (ENaC) and cystic
fibrosis transmembrane conductance regulator (CFTR) are co-localized in
the apical membrane of many epithelia. These channels are essential for
electrolyte and water secretion and/or reabsorption. In cystic fibrosis
airway epithelia, a hyperactivated epithelial Na+
conductance operates in parallel with defective Cl
The Cytosolic Termini of the
- and 
-ENaC Subunits Are
Involved in the Functional Interactions between Cystic Fibrosis
Transmembrane Conductance Regulator and Epithelial Sodium
Channel*
,,,,,¶
Department of Physiology and Biophysics,
University of Alabama at Birmingham, Birmingham, Alabama 35294-0005 and
the § Department of Physiology, Dartmouth Medical School,
Hanover, New Hampshire 03755
secretion. Several groups have shown that CFTR down-regulates ENaC
activity, but the mechanisms and the regulation of CFTR by ENaC are
unknown. To test the hypothesis that ENaC and CFTR regulate each other,
and to identify the region(s) of ENaC involved in the interaction
between CFTR and ENaC, rENaC and its mutants were co-expressed with
CFTR in Xenopus oocytes. Whole cell macroscopic sodium
currents revealed that wild type (wt) 
-rENaC-induced Na+ current was inhibited by co-expression of CFTR, and
further inhibited when CFTR was activated with a cAMP-raising mixture
(CKT). Conversely, -rENaC stimulated CFTR-mediated
Cl currents up to ~6-fold. Deletion mutations in the
intracellular tails of the three rENaC subunits suggested that the
carboxyl terminus of the subunit was required both for the
down-regulation of ENaC by activated CFTR and the up-regulation of CFTR
by ENaC. However, both the carboxyl terminus of the subunit and the
amino terminus of the subunit were essential for the
down-regulation of rENaC by unstimulated CFTR. Interestingly,
down-regulation of rENaC by activated CFTR was
Cl-dependent, while stimulation of CFTR by
rENaC was not dependent on either cytoplasmic Na+ or a
depolarized membrane potential. In summary, there appear to be at least
two different sites in ENaC involved in the intermolecular interaction
between CFTR and ENaC.
*
This work was supported by National Institutes of Health
Grants DK45881, DK51067, DK53090 and the Cystic Fibrosis Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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