Journal article
The amino-terminal portion of CFTR forms a regulated Cl- channel
Cell (Cambridge), Vol.76(6), pp.1091-1098
03/25/1994
DOI: 10.1016/0092-8674(94)90385-9
PMID: 7511062
Abstract
The cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channel consists of two motifs (each containing a membrane-spanning domain [MSD] and a nucleotide-binding domain [NBD]) linked by an R domain. We tested the hypothesis that one MSD-NBD motif could form a Cl- channel. The amino-terminal portion of CFTR (D836X, which contains MSD1, NBD1, and the R domain) formed Cl- channels with conductive properties identical to those of CFTR. However, channel regulation differed. Although phosphorylation increased activity, channels opened without phosphorylation. MgATP stimulated D836X more potently than CFTR and may interact at more than one site. These data and migration of D836X on sucrose density gradients suggest that D836X may function as a multimer. Thus, the amino-terminal portion of CFTR contains all of the structures required to build a regulated Cl- channel.
Details
- Title: Subtitle
- The amino-terminal portion of CFTR forms a regulated Cl- channel
- Creators
- D N Sheppard - Howard Hughes Medical Institute, Department of Internal Medicine, University of Iowa College of Medicine, Iowa City 52242L S OstedgaardD P RichM J Welsh
- Resource Type
- Journal article
- Publication Details
- Cell (Cambridge), Vol.76(6), pp.1091-1098
- Publisher
- United States
- DOI
- 10.1016/0092-8674(94)90385-9
- PMID
- 7511062
- ISSN
- 0092-8674
- eISSN
- 1097-4172
- Language
- English
- Date published
- 03/25/1994
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Pulmonary, Critical Care, and Occupational Medicine; Fraternal Order of Eagles Diabetes Research Center; Neurosurgery; Internal Medicine
- Record Identifier
- 9984020996402771
Metrics
18 Record Views