The cystic fibrosis mutation (ΔF508) does not influence the chloride channel activity of CFTR
Authors:
- Mohabir RamjeesinghMRMohabir Ramjeesingh
- Evangelica ReyesEREvangelica Reyes
- Tim JensenTJTim Jensen
- Xiubao ChangXCXiubao Chang
- Johanna M. RommensJRJohanna M. Rommens
- Christine E. BearCBChristine E. Bear
- 1 April 1993
- journal article
- Published by Springer Nature in Nature Genetics
- Vol. 3 (4) , 311-316
Abstract
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.Keywords
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