[HTML][HTML] Conformational and temperature-sensitive stability defects of the ΔF508 cystic fibrosis transmembrane conductance regulator in post-endoplasmic reticulum …
Deletion of phenylalanine at position 508 (ΔF508) is the most common cystic fibrosis (CF)-
associated mutation in the CF transmembrane conductance regulator (CFTR), a cAMP-
regulated chloride channel. The consensus notion is that ΔF508 imposes a temperature-
sensitive folding defect and targets newly synthesized CFTR for degradation at endoplasmic
reticulum (ER). A limited amount of CFTR activity, however, appears at the cell surface in the
epithelia of homozygous ΔF508 CFTR mice and patients, suggesting that the ER retention is …
associated mutation in the CF transmembrane conductance regulator (CFTR), a cAMP-
regulated chloride channel. The consensus notion is that ΔF508 imposes a temperature-
sensitive folding defect and targets newly synthesized CFTR for degradation at endoplasmic
reticulum (ER). A limited amount of CFTR activity, however, appears at the cell surface in the
epithelia of homozygous ΔF508 CFTR mice and patients, suggesting that the ER retention is …
