The cystic fibrosis transmembrane conductance regulator (CFTR) is mutated in patients with cystic fibrosis (CF). The most common CF-associated mutation is deletion of phenylanine at residue 508, CFTRΔF508. When expressed in heterologous cells, CFTR bearing the ΔF508 mutation fails to progress through the normal biosynthetic pathway and fails to traffic to the plasma membrane. As a result, CFTRΔF508 is mislocalized and is not present in the apical membrane of primary cultures of airway epithelia. Consequently, the apical membrane of CF airway epithelia is Cl--impermeable, a defect that probably contributes to the pathogenesis of the disease.
Mendeley helps you to discover research relevant for your work.
CITATION STYLE
Welsh, M. J., Denning, G. M., Ostedgaard, L. S., & Anderson, M. P. (1993). Dysfunction of CFTR bearing the ΔF508 mutation. In Journal of Cell Science (Vol. 106, pp. 235–239). Company of Biologists Ltd. https://doi.org/10.1242/jcs.1993.supplement_17.33