Exploiting species differences to understand the CFTR Cl- channel

Sam Bose, Toby Scott-Ward, Zhiwei Cai, David Sheppard

Research output: Contribution to journalArticle (Academic Journal)peer-review

12 Citations (Scopus)
411 Downloads (Pure)


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 impact strongly on channel function and the action of CF mutations.
Original languageEnglish
Pages (from-to)975-982
Number of pages8
JournalBiochemical Society Transactions
Issue number5
Publication statusPublished - 1 Oct 2015


  • ATP-binding cassette transporte
  • ystic fibrosis transmembrane conductance regulator (CFTR)
  • chloride ion channel
  • cystic fibrosis
  • 508del–CFTR
  • CFTR pharmacology


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