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J Biol Chem, Vol. 274, Issue 43, 30345-30348, October 22, 1999
COMMUNICATION
Regulation of the Amiloride-sensitive Epithelial Sodium Channel
by Syntaxin 1A
Juanjuan
Qi,
Kathryn W.
Peters,
Chongguang
Liu,
Jun-Min
Wang,
Robert S.
Edinger,
John P.
Johnson,
Simon C.
Watkins, and
Raymond A.
Frizzell
From the Departments of Cell Biology and Physiology and Medicine,
University of Pittsburgh School of Medicine,
Pittsburgh, Pennsylvania 15261
The first step in transepithelial sodium
absorption lies at the apical membrane where the amiloride-sensitive,
epithelial sodium channel, ENaC, facilitates sodium entry into the
cell. Here we report that the vesicle traffic regulatory (SNARE
(soluble N-ethylmaleimide-sensitive factor attachment
protein receptor)) protein, syntaxin 1A (S1A), inhibits ENaC mediated
sodium entry. This inhibitory effect is selective for S1A and is not
reproduced by syntaxin 3. The inhibition does not require the membrane
anchoring domain of syntaxin 1A. It was reversed by the S1A-binding
protein, Munc-18, but not by a Munc-18 mutant, which lacks syntaxin
affinity. Immunostaining of epitope-tagged ENaC subunits showed that
syntaxin 1A decreases ENaC current by reducing the number of ENaC
channels in the plasma membrane; S1A does not interfere with ENaC
protein expression. Immunoprecipitation of syntaxin 1A from the
sodium-transporting epithelial cell line, A6, co-precipitates ENaC.
These findings indicate that syntaxin 1A and other members of the SNARE
machinery are involved in the control of plasma membrane ENaC content,
and they suggest that SNARE proteins participate in the regulation of
sodium absorption in relation to agonist mediated vesicle
insertion-retrieval processes.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
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