Clathrin-mediated endocytosis of the epithelial sodium channel. Role of epsin.

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 sub-domains acted as dominant-negative effectors and stimulated ENaC activity. These results identify epsin as an accessory protein linking ENaC to the clathrin-based endocytic machinery thereby regulating the activity of this ion channel at the cell surface.
Mesh Terms:
Adaptor Proteins, Vesicular Transport, Animals, Cell Membrane, Clathrin, Down-Regulation, Electrophysiology, Endocytosis, Endosomes, Mice, Mutation, Oocytes, Protein Structure, Tertiary, Ubiquitin, Xenopus
J. Biol. Chem.
Date: May. 19, 2006
Download Curated Data For This Publication
101587
Switch View:
  • Interactions 9
  • PTM Genes 4