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- Title
CFTR chloride channel regulation by an interdomain interaction.
- Authors
Naren, A P; Cormet-Boyaka, E; Fu, J; Villain, M; Blalock, J E; Quick, M W; Kirk, K L
- Abstract
The cystic fibrosis gene encodes a chloride channel, CFTR (cystic fibrosis transmembrane conductance regulator), that regulates salt and water transport across epithelial tissues. Phosphorylation of the cytoplasmic regulatory (R) domain by protein kinase A activates CFTR by an unknown mechanism. The amino-terminal cytoplasmic tail of CFTR was found to control protein kinase A-dependent channel gating through a physical interaction with the R domain. This regulatory activity mapped to a cluster of acidic residues in the NH(2)-terminal tail; mutating these residues proportionately inhibited R domain binding and CFTR channel function. CFTR activity appears to be governed by an interdomain interaction involving the amino-terminal tail, which is a potential target for physiologic and pharmacologic modulators of this ion channel.
- Publication
Science (New York, N.Y.), 1999, Vol 286, Issue 5439, p544
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.286.5439.544