Cystic fibrosis transmembrane conductance regulator (CFTR): Making an ion channel out of an active transporter structure. Issue 1 (1st January 2018)

• Record Type: Journal Article
• Authors: Linsdell, Paul
• Is Part Of: Channels. Volume 12:Issue 1(2018)
• Page Start: 284
• Page End: 290
• Publication Date: 2018-01-01
• Subjects: ABC protein -- CFTR -- channel pore -- chloride channel -- cystic fibrosis -- ion channel; Ion channels -- Periodicals; 572.3
• DOI: 10.1080/19336950.2018.1502585
• Languages: English
• ISSNs: 1933-6950

Abstract

ABSTRACT: Cystic fibrosis is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR). CFTR is a member of the ATP-binding cassette (ABC) family of membrane transport proteins, most members of which function as ATP-dependent pumps. CFTR is unique among human ABC proteins in functioning not as a pump, but as an ion channel. Recent structural data has indicated that CFTR shares broadly similar overall architecture and ATP-dependent conformational changes as other ABC proteins. Functional investigations suggest that CFTR has a unique open portal connecting the cytoplasm to the transmembrane channel pore, that allows for a continuous pathway for Cl − ions to cross the membrane in one conformation. This lateral portal may be what allows CFTR to function as an ion channel rather than as a pump, suggesting a plausible mechanism by which channel function may have evolved in CFTR.