F508del CFTR with two altered RXR motifs escapes from ER quality control but its channel activity is thermally sensitive.

@article{Hegeds2006F508delCW,
  title={F508del CFTR with two altered RXR motifs escapes from ER quality control but its channel activity is thermally sensitive.},
  author={Tam{\'a}s Hegedűs and Andrei A. Aleksandrov and Li-ying Cui and Martina Gentzsch and Xiu-bao Chang and John R. Riordan},
  journal={Biochimica et biophysica acta},
  year={2006},
  volume={1758 5},
  pages={565-72}
}
Most cystic fibrosis (CF) patients carry the F508del mutation in the CFTR chloride channel protein resulting in its misassembly, retention in the endoplasmic reticulum (ER), and proteasomal degradation. Therefore, characterization of the retention and attempts to rescue the mutant CFTR are a major focus of CF research. Earlier, we had shown that four arginine-framed tripeptide (AFT) signals in CFTR participate in the quality control. Now we have mutated these four AFTs in all possible… CONTINUE READING