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PMID:10642508

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Citation

Farr, TJ, Coddington-Lawson, SJ, Snyder, PM and McDonald, FJ (2000) Human Nedd4 interacts with the human epithelial Na+ channel: WW3 but not WW1 binds to Na+-channel subunits. Biochem. J. 345 Pt 3:503-9

Abstract

The epithelial Na(+) channel (ENaC) regulates Na(+) absorption in epithelial tissues including the lung, colon and sweat gland, and in the distal nephrons of the kidney. When Na(+)-channel function is disrupted, salt and water homoeostasis is affected. The cytoplasmic regions of the Na(+)-channel subunits provide binding sites for other proteins to interact with and potentially regulate Na(+)-channel activity. Previously we showed that a proline-rich region of the alpha subunit of the Na(+) channel bound to a protein of 116 kDa from human lung cells. Here we report the identification of this protein as human Nedd4, a ubiquitin-protein ligase that binds to the Na(+)-channel subunits via its WW domains. Further, we show that WW domains 2, 3 and 4 of human Nedd4 bind to the alpha, beta and gamma Na(+)-channel subunits but not to a mutated beta subunit. In addition, when co-expressed in Xenopus oocytes, human Nedd4 down-regulates Na(+)-channel activity.

Links

PubMed PMC1220784

Keywords

Amino Acid Motifs; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; COS Cells/metabolism; Calcium-Binding Proteins/genetics; Calcium-Binding Proteins/metabolism; Cloning, Molecular; Dogs; Endosomal Sorting Complexes Required for Transport; Epithelial Sodium Channel; Humans; Ligases; Molecular Sequence Data; Oocytes/metabolism; RNA, Messenger; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Sequence Homology, Amino Acid; Sodium Channels/metabolism; Ubiquitin-Protein Ligases; Xenopus; src Homology Domains

Significance

Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status


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References

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