Journal article
Electrophysiological and Biochemical Evidence That DEG/ENaC Cation Channels Are Composed of Nine Subunits
The Journal of biological chemistry, Vol.273(2), pp.681-684
01/09/1998
DOI: 10.1074/jbc.273.2.681
PMID: 9422716
Abstract
Members of the DEG/ENaC protein family form ion channels with diverse functions. DEG/ENaC subunits associate as hetero- and homomultimers to generate channels; however the stoichiometry of these complexes is unknown. To determine the subunit stoichiometry of the human epithelial Na+ channel (hENaC), we expressed the three wild-type hENaC subunits (alpha, beta, and gamma) with subunits containing mutations that alter channel inhibition by methanethiosulfonates. The data indicate that hENaC contains three alpha, three beta, and three gamma subunits. Sucrose gradient sedimentation of alphahENaC translated in vitro, as well as alpha-, beta-, and gammahENaC coexpressed in cells, was consistent with complexes containing nine subunits. FaNaCh and BNC1, two related DEG/ENaC channels, produced complexes of similar mass. Our results suggest a novel nine-subunit stoichiometry for the DEG/ENaC family of ion channels.
Details
- Title: Subtitle
- Electrophysiological and Biochemical Evidence That DEG/ENaC Cation Channels Are Composed of Nine Subunits
- Creators
- Peter M SnyderChun ChengLawrence S PrinceJohn C RogersMichael J Welsh
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.273(2), pp.681-684
- DOI
- 10.1074/jbc.273.2.681
- PMID
- 9422716
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Language
- English
- Date published
- 01/09/1998
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Pulmonary, Critical Care, and Occupational Medicine; Cardiovascular Medicine; Neurosurgery; Medicine Administration; Internal Medicine
- Record Identifier
- 9984020884002771
Metrics
17 Record Views