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XB-ART-44616
J Biol Chem 2011 Sep 16;28637:31944-52. doi: 10.1074/jbc.M111.275289.
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Atomic force microscopy reveals the architecture of the epithelial sodium channel (ENaC).

Stewart AP , Haerteis S , Diakov A , Korbmacher C , Edwardson JM .


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The epithelial sodium channel (ENaC) is a member of the ENaC/degenerin superfamily. ENaC is a heteromultimer containing three homologous subunits (α, β, and γ); however, the subunit stoichiometry is still controversial. Here, we addressed this issue using atomic force microscopy imaging of complexes between isolated ENaC and antibodies/Fab fragments directed against specific epitope tags on the α-, β- and γ-subunits. We show that for α-, β- and γ-ENaC alone, pairs of antibodies decorate the channel at an angle of 120°, indicating that the individual subunits assemble as homotrimers. A similar approach demonstrates that αβγ-ENaC assembles as a heterotrimer containing one copy of each subunit. Intriguingly, all four subunit combinations also produce higher-order structures containing two or three individual trimers. The trimer-of-trimers organization would account for earlier reports that ENaC contains eight to nine subunits.

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References [+] :
Anantharam, Determination of epithelial Na+ channel subunit stoichiometry from single-channel conductances. 2007, Pubmed, Xenbase