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ATPase activity of the cystic fibrosis transmembrane conductance regulator
- Source :
- The Journal of biological chemistry. 271(45)
- Publication Year :
- 1996
-
Abstract
- The gene mutated in cystic fibrosis codes for the cystic fibrosis transmembrane conductance regulator (CFTR), a cyclic AMP-activated chloride channel thought to be critical for salt and water transport by epithelial cells. Plausible models exist to describe a role for ATP hydrolysis in CFTR channel activity; however, biochemical evidence that CFTR possesses intrinsic ATPase activity is lacking. In this study, we report the first measurements of the rate of ATP hydrolysis by purified, reconstituted CFTR. The mutation CFTRG551D resides within a motif conserved in many nucleotidases and is known to cause severe human disease. Following reconstitution the mutant protein exhibited both defective ATP hydrolysis and channel gating, providing direct evidence that CFTR utilizes ATP to gate its channel activity.
- Subjects :
- congenital, hereditary, and neonatal diseases and abnormalities
Cystic Fibrosis Transmembrane Conductance Regulator
Biochemistry
Cystic fibrosis
Nucleotidases
Adenosine Triphosphate
ATP hydrolysis
Mutant protein
Chloride Channels
medicine
Humans
Phosphorylation
Molecular Biology
Adenosine Triphosphatases
Water transport
biology
Chemistry
Hydrolysis
Cell Biology
medicine.disease
Cyclic AMP-Dependent Protein Kinases
Cystic fibrosis transmembrane conductance regulator
Recombinant Proteins
Cell biology
Kinetics
Chloride channel
biology.protein
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 271
- Issue :
- 45
- Database :
- OpenAIRE
- Journal :
- The Journal of biological chemistry
- Accession number :
- edsair.doi.dedup.....711e58ad51f4cf086ace94a7b734abd0