Article
Role of CFTR's PDZ1-binding domain, NBF1 and Cl(-) conductance in inhibition of epithelial Na(+) channels in Xenopus oocytes.
Biochimica et biophysica acta - 1 Nov 2001
Boucherot A, Schreiber R, Kunzelmann K
Abstract excerpt
The cystic fibrosis transmembrane conductance regulator (CFTR) inhibits epithelial Na(+) channels (ENaC). Evidence has accumulated that both Cl(-) transport through CFTR Cl(-) channels and the first nucleotide binding domain (NBF1) of CFTR are crucial for inhibition of ENaC. A PDZ binding domain (PDZ-BD) at the C-terminal end links CFTR to scaffolding and cytoskeletal proteins, which have been suggested to play...
Topics
- Animals
- Binding Sites
- Bromides
- Cells, Cultured
- Chloride Channels
- Chlorides
- Cystic Fibrosis Transmembrane Conductance Regulator
- Electrochemistry
- Epithelium
- Gene Expression Regulation
- Iodides
- Mutation
- Oocytes
- Sodium Channel Blockers
- Sodium Channels
- Transfection
- Xenopus