Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Nedd4-2 catalyzes ubiquitination and degradation of cell surface ENaC.

The Journal of biological chemistry - 13 Jul 2007

Zhou Ruifeng, Patel Saumil V, Snyder Peter M

Abstract excerpt

Epithelial Na(+) absorption is regulated by Nedd4-2, an E3 ubiquitin-protein ligase that reduces expression of the epithelial Na(+) channel ENaC at the cell surface. Defects in this regulation cause Liddle syndrome, an inherited form of hypertension. Previous work found that Nedd4-2 binds to ENaC via PY motifs located in the C termini of alpha-, beta-, and gammaENaC. However, little is known about the mechanism...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Epithelial Sodium Channels
Share to Endosomal Sorting Complexes Required for Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Silencing

Share to Ion Transport

Share to Nedd4 Ubiquitin Protein Ligases

Share to Protein Processing, Post-Translational

Share to Sodium

Share to Ubiquitin

Source

Identifiers

PMID: 17502380
DOI: 10.1074/jbc.M611329200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nedd4-2 catalyzes ubiquitination and degradation of cell surface ENaC.PMID 17502380Read ↗

Participation of the ubiquitin-conjugating enzyme UBE2E3 in Nedd4-2-dependent regulation of the epithelial Na+ channel.Semantic proximity Read ↗

Liddle's syndrome mutations increase Na+ transport through dual effects on epithelial Na+ channel surface expression and proteolytic cleavage.Semantic proximity Read ↗

Defective regulation of the epithelial Na+ channel by Nedd4 in Liddle's syndrome.Semantic proximity Read ↗

Regulation of stability and function of the epithelial Na+ channel (ENaC) by ubiquitination.Semantic proximity Read ↗

WNK4 inhibition of ENaC is independent of Nedd4-2-mediated ENaC ubiquitination.Semantic proximity Read ↗

Hrs controls sorting of the epithelial Na+ channel between endosomal degradation and recycling pathways.Semantic proximity Read ↗

Nedd4-2 phosphorylation induces serum and glucocorticoid-regulated kinase (SGK) ubiquitination and degradation.Semantic proximity Read ↗

A novel mouse Nedd4 protein suppresses the activity of the epithelial Na+ channel.Semantic proximity Read ↗

Multiple WW domains, but not the C2 domain, are required for inhibition of the epithelial Na+ channel by human Nedd4.Semantic proximity Read ↗

Regulation of the Na-K-2Cl cotransporter NKCC2 by ubiquitylationSemantic proximity Read ↗

The PY motif of ENaC, mutated in Liddle syndrome, regulates channel internalization, sorting and mobilization from subapical pool.Semantic proximity Read ↗

Alternate promoters and variable splicing lead to hNedd4-2 isoforms with a C2 domain and varying number of WW domains.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.