Journal article
Structure and Function of the CFTR Chloride Channel
Physiological reviews, Vol.79(1), pp.S23-S45
01/01/1999
DOI: 10.1152/physrev.1999.79.1.S23
PMID: 9922375
Abstract
Sheppard, David N., and Michael J. Welsh. Structure and Function of the CFTR Chloride Channel. Physiol. Rev. 79 , Suppl.: S23–S45, 1999. — The cystic fibrosis transmembrane conductance regulator (CFTR) is a unique member of the ABC transporter family that forms a novel Cl− channel. It is located predominantly in the apical membrane of epithelia where it mediates transepithelial salt and liquid movement. Dysfunction of CFTR causes the genetic disease cystic fibrosis. The CFTR is composed of five domains: two membrane-spanning domains (MSDs), two nucleotide-binding domains (NBDs), and a regulatory (R) domain. Here we review the structure and function of this unique channel, with a focus on how the various domains contribute to channel function. The MSDs form the channel pore, phosphorylation of the R domain determines channel activity, and ATP hydrolysis by the NBDs controls channel gating. Current knowledge of CFTR structure and function may help us understand better its mechanism of action, its role in electrolyte transport, its dysfunction in cystic fibrosis, and its relationship to other ABC transporters.
Details
- Title: Subtitle
- Structure and Function of the CFTR Chloride Channel
- Creators
- DAVID N. Sheppard - Western General HospitalMICHAEL J. Welsh - University of Iowa
- Resource Type
- Journal article
- Publication Details
- Physiological reviews, Vol.79(1), pp.S23-S45
- DOI
- 10.1152/physrev.1999.79.1.S23
- PMID
- 9922375
- NLM abbreviation
- Physiol Rev
- ISSN
- 0031-9333
- eISSN
- 1522-1210
- Language
- English
- Date published
- 01/01/1999
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Pulmonary, Critical Care, and Occupational Medicine; Fraternal Order of Eagles Diabetes Research Center; Neurosurgery; Internal Medicine
- Record Identifier
- 9984259504202771
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