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Papers In Press, published online ahead of print March 30, 2006
Medicine Dept., University of Pittsburgh, Pittsburgh, PA 15261
Corresponding Author: johnson{at}dom.pitt.edu
Here we present evidence that the epithelial sodium channel (ENaC), a heteromeric membrane protein whose surface expression is regulated by ubiquitination, is present in clathrin-coated vesicles in epithelial cells that natively express ENaC. The channel subunits are ubiquitinated and co-immunoprecipitate with both epsin and clathrin adaptor proteins, and epsin, as expected, co-immunoprecipitates with clathrin adaptor proteins. The functional significance of these interactions was evaluated in a Xenopus oocyte expression system where co-expression of epsin and ENaC resulted in a down-regulation of ENaC activity; conversely, co-expression of epsin domains acted as dominant-negatives and stimulated ENaC activity. These results identify epsin as an accessory protein linking ENaC to clathrin-based endocytic machinery thereby regulating the activity of this ion channel.
J. Biol. Chem, 10.1074/jbc.M512511200
Submitted on November 22, 2005
Accepted on March 30, 2006
Clathrin-mediated endocytosis of ENaC: Role of epsin
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