Article
Severed channels probe regulation of gating of cystic fibrosis transmembrane conductance regulator by its cytoplasmic domains.
The Journal of general physiology - 1 Sept 2000
Csanády L, Chan K W, Seto-Young D, Kopsco D C, Nairn A C, Gadsby D C
Abstract excerpt
Opening and closing of a CFTR Cl(-) channel is controlled by PKA-mediated phosphorylation of its cytoplasmic regulatory (R) domain and by ATP binding, and likely hydrolysis, at its two nucleotide binding domains. Functional interactions between the R domain and the two nucleotide binding domains were probed by characterizing the gating of severed CFTR channels expressed in Xenopus oocytes. Expression levels were...
Topics
- Adenosine Triphosphate
- Adenylyl Imidodiphosphate
- Animals
- Base Sequence
- Cyclic AMP-Dependent Protein Kinases
- Cystic Fibrosis
- Cystic Fibrosis Transmembrane Conductance Regulator
- DNA Primers
- Female
- Humans
- In Vitro Techniques
- Ion Channel Gating
- Models, Biological