Journal article
An Intrinsic Adenylate Kinase Activity Regulates Gating of the ABC Transporter CFTR
Cell (Cambridge), Vol.115(7), pp.837-850
12/26/2003
DOI: 10.1016/S0092-8674(03)00983-8
PMID: 14697202
Abstract
Cystic fibrosis transmembrane conductance regulator (CFTR) is an anion channel in the ATP binding cassette (ABC) transporter family. Like other ABC transporters, it can hydrolyze ATP. Yet while ATP hydrolysis influences channel gating, it has long seemed puzzling that CFTR would require this reaction because anions flow passively through CFTR. Moreover, no other ion channel is known to require the large energy of ATP hydrolysis to gate. We found that CFTR also has adenylate kinase activity (ATP + AMP ←⃗ ADP + ADP) that regulates gating. When functioning as an adenylate kinase, CFTR showed positive cooperativity for ATP suggesting its two nucleotide binding domains may dimerize. Thus, channel activity could be regulated by two different enzymatic reactions, ATPase and adenylate kinase, that share a common ATP binding site in the second nucleotide binding domain. At physiologic nucleotide concentrations, adenylate kinase activity, rather than ATPase activity may control gating, and therefore involve little energy consumption.
Details
- Title: Subtitle
- An Intrinsic Adenylate Kinase Activity Regulates Gating of the ABC Transporter CFTR
- Creators
- Christoph RandakMichael J Welsh
- Resource Type
- Journal article
- Publication Details
- Cell (Cambridge), Vol.115(7), pp.837-850
- Publisher
- Elsevier Inc
- DOI
- 10.1016/S0092-8674(03)00983-8
- PMID
- 14697202
- ISSN
- 0092-8674
- eISSN
- 1097-4172
- Language
- English
- Date published
- 12/26/2003
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Pulmonary, Critical Care, and Occupational Medicine; Pulmonary Medicine; Stead Family Department of Pediatrics; Neurosurgery; Internal Medicine
- Record Identifier
- 9984020849202771
Metrics
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