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The anion channel cystic fibrosis transmembrane conductance regulator (CFTR) is a unique ATP-binding cassette (ABC) transporter. CFTR plays a pivotal role in transepithelial ion transport as its dysfunction in the genetic disease cystic fibrosis (CF) dramatically demonstrates. Phylogenetic analysis suggests that CFTR first appeared in aquatic vertebrates fulfilling important roles in osmosensing and organ development. Here, we review selectively, knowledge of CFTR structure, function and pharmacology, gleaned from cross-species comparative studies of recombinant CFTR proteins, including CFTR chimeras. The data argue that subtle changes in CFTR structure can affect strongly channel function and the action of CF mutations.

Original publication

DOI

10.1042/BST20150129

Type

Journal article

Journal

Biochem Soc Trans

Publication Date

10/2015

Volume

43

Pages

975 - 982

Keywords

ATP-binding cassette transporter, CFTR pharmacology, F508del–CFTR, chloride ion channel, cystic fibrosis, cystic fibrosis transmembrane conductance regulator (CFTR), Adenosine Monophosphate, Adenosine Triphosphate, Animals, Cystic Fibrosis, Cystic Fibrosis Transmembrane Conductance Regulator, Humans, Ion Channel Gating, Mutation, Phylogeny, Species Specificity