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

Proteolytic processing of the epithelial sodium channel gamma subunit has a dominant role in channel activation.

The Journal of biological chemistry - 12 Sept 2008

Carattino Marcelo D, Hughey Rebecca P, Kleyman Thomas R

Abstract excerpt

Maturation of the epithelial sodium channel (ENaC) involves furin-dependent cleavage at two extracellular sites within the alpha subunit and at a single extracellular site within the gamma subunit. Channels lacking furin processing of the alpha subunit have very low activity. We recently identified a prostasin-dependent cleavage site (RKRK(186)) in the gamma subunit. We also demonstrated that the tract alpha...

Read the complete abstract on PubMed

Topics

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

Share to Electrophysiology
Share to Epithelial Sodium Channels

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oocytes

Share to Patch-Clamp Techniques

Share to RNA, Complementary

Share to Serine Endopeptidases

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 18650438
DOI: 10.1074/jbc.M803931200
PMCID: PMC2533072

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Proteolytic processing of the epithelial sodium channel gamma subunit has a dominant role in channel activation.PMID 18650438Read ↗

Cleavage in the {gamma}-subunit of the epithelial sodium channel (ENaC) plays an important role in the proteolytic activation of near-silent channels.Semantic proximity Read ↗

Influence of proteolytic cleavage of ENaC's γ subunit upon Na+ and K+ handling.Semantic proximity Read ↗

Functional expression of a pseudohypoaldosteronism type I mutated epithelial Na+ channel lacking the pore-forming region of its α subunitSemantic proximity Read ↗

A mutation of the epithelial sodium channel associated with atypical cystic fibrosis increases channel open probability and reduces Na+ self inhibition.Semantic proximity Read ↗

Gamma subunit second transmembrane domain contributes to epithelial sodium channel gating and amiloride block.Semantic proximity Read ↗

Functional characterization of a partial loss-of-function mutation of the epithelial sodium channel (ENaC) associated with atypical cystic fibrosis.Semantic proximity Read ↗

A mutation in the epithelial sodium channel causing Liddle disease increases channel activity in the Xenopus laevis oocyte expression system.Semantic proximity Read ↗

Proteolytic activation of the epithelial sodium channel (ENaC) in health and disease.Semantic proximity Read ↗

Stimulation of the epithelial sodium channel (ENaC) by cAMP involves putative ERK phosphorylation sites in the C termini of the channel's beta- and gamma-subunit.Semantic proximity Read ↗

Novel determinants of epithelial sodium channel gating within extracellular thumb domains.Semantic proximity Read ↗

Multiple epithelial Na+ channel domains participate in subunit assembly.Semantic proximity Read ↗

Proteolytic activation of the human epithelial sodium channel by trypsin IV and trypsin I involves distinct cleavage sites.Semantic proximity Read ↗

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