The cystic fibrosis mutation (ΔF508) does not influence the chloride channel activity of CFTR

Canhui Li, Mohabir Ramjeesingh, Evangelica Reyes, Tim Jensen, Xiubao Chang, Johanna M. Rommens, Christine E. Bear

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Abstract

The cystic fibrosis transmembrane conductance regulator (CFTR) is a phosphorylation-regulated Ch channel. In most mammalian cells, the functional consequences of the most common CF mutation, ΔF508-CFTR, cannot be assessed as the mutant protein undergoes biosynthetic arrest. However, function can be studied in the baculovirus-insect cell expression system where ΔF508-CFTR does not appear to undergo such arrest. Our results show that phosphorylation-regulated Cl channel activity of ΔF508-CFTR is similar to that of wild-type CFTR. This observation was confirmed in comparative studies of purified ΔF508-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.

Original languageEnglish (US)
Pages (from-to)311-316
Number of pages6
JournalNature Genetics
Volume3
Issue number4
DOIs
StatePublished - Apr 1993

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ASJC Scopus subject areas

  • Genetics

Cite this

Li, C., Ramjeesingh, M., Reyes, E., Jensen, T., Chang, X., Rommens, J. M., & Bear, C. E. (1993). The cystic fibrosis mutation (ΔF508) does not influence the chloride channel activity of CFTR. Nature Genetics, 3(4), 311-316. https://doi.org/10.1038/ng0493-311