The cystic fibrosis mutation (delta F508) does not influence the chloride channel activity of CFTR

Nat Genet. 1993 Apr;3(4):311-6. doi: 10.1038/ng0493-311.


The cystic fibrosis transmembrane conductance regulator (CFTR) is a phosphorylation-regulated Cl- channel. In most mammalian cells, the functional consequences of the most common CF mutation, delta F508-CFTR, cannot be assessed as the mutant protein undergoes biosynthetic arrest. However, function can be studied in the baculovirus-insect cell expression system where delta F508-CFTR does not appear to undergo such arrest. Our results show that phosphorylation-regulated Cl- channel activity of delta F508-CFTR is similar to that of wild-type CFTR. This observation was confirmed in comparative studies of purified delta F508-CFTR and CFTR reconstituted in planar lipid bilayers. Therefore, we suggest that this common mutation does not result in a significant alteration in CFTR function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • CHO Cells
  • Cell Line
  • Chloride Channels / chemistry
  • Chloride Channels / genetics*
  • Chloride Channels / metabolism
  • Cricetinae
  • Cyclic AMP / pharmacology
  • Cystic Fibrosis / genetics*
  • Cystic Fibrosis Transmembrane Conductance Regulator
  • Humans
  • Kinetics
  • Lipid Bilayers
  • Membrane Potentials / drug effects
  • Membrane Potentials / physiology
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Phenylalanine*
  • Phosphorylation
  • Protein Folding
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Deletion*
  • Spodoptera
  • Transfection


  • CFTR protein, human
  • Chloride Channels
  • Lipid Bilayers
  • Membrane Proteins
  • Recombinant Proteins
  • Cystic Fibrosis Transmembrane Conductance Regulator
  • Phenylalanine
  • Cyclic AMP