CFTR is a monomer: Biochemical and functional evidence

J. H. Chen, X. B. Chang, A. A. Aleksandrov, J. R. Riordan

Research output: Contribution to journalArticlepeer-review

33 Scopus citations


Although the CFTR protein alone is sufficient to generate a regulated chloride channel, it is unknown how many of the polypeptides form the channel. Using biochemical and functional assays, we demonstrate that the CFTR polypeptide is a monomer. CFTR sediments as a monomer in a linear, continuous sucrose gradient. Cells co-expressing different epitope-tagged CFTR provide no evidence of co-assembly in immunoprecipitation and nickel affinity binding experiments. Co-expressed wild-type and ΔF508 CFTR are without influence on each other in their ability to progress through the secretory pathway, suggesting they do not associate in the endoplasmic reticulum. No hybrid conducting single channels are seen in planar lipid bilayers with which membrane vesicles from cells co-expressing similar amounts of two different CFTR conduction species have been fused.

Original languageEnglish (US)
Pages (from-to)55-71
Number of pages17
JournalJournal of Membrane Biology
Issue number1
StatePublished - Jul 1 2002


  • ABC protein
  • CFTR
  • CFTR monomer
  • Chloride channel
  • Cystic fibrosis
  • Quaternary structure

ASJC Scopus subject areas

  • Biophysics
  • Physiology
  • Cell Biology


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