期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 286, 期 37, 页码 31944-31952出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.275289
关键词
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资金
- Jean Shanks Foundation
- James Baird Fund
- IZKF (Interdisciplinary Centre of Clinical Research)
- Friedrich-Alexander-Universitat Erlangen-Nurnberg
- Bayerische Forschungsstiftung
- Deutsche Forschungsgemeinschaft [SFB 423, A12]
- Kidney Research UK
- Kidney Research UK [RP11/2009] Funding Source: researchfish
The epithelial sodium channel (ENaC) is a member of the ENaC/degenerin superfamily. ENaC is a heteromultimer containing three homologous subunits (alpha, beta, and gamma); 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 alpha-, beta- and gamma-subunits. We show that for alpha-, beta- and gamma-ENaC alone, pairs of antibodies decorate the channel at an angle of 120 degrees, indicating that the individual subunits assemble as homotrimers. A similar approach demonstrates that alpha beta gamma-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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