More than 1,300 different mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) are the cause for cystic fibrosis. CFTR is in charge of proper secretion and absorption of electrolytes, and thus the disease is characterized by defective epithelial Cl(-) secretion and enhanced Na(+) absorption. Recent studies show that CFTR interacts with other proteins via PDZ domains.

Ivacaftor, a cystic fibrosis transmembrane conductance regulator (CFTR) potentiator, is approved for the treatment of patients with cystic fibrosis (CF) with the G551D mutation aged 6 years or older. To evaluate the efficacy of this CFTR-modulating therapy (CFTR-MT) biomarkers such as sweat chloride (SC), nasal potential difference (NPD) and intestinal current measurement (ICM) have been implem...

The folding, misfolding, and degradation of membrane proteins is controlled by multiple processes within the cell. In this issue of Cell, Wang et al. (2006) present an interactome for CFTR, the chloride channel that is misfolded and prematurely degraded in cystic fibrosis. Among the proteins interacting with CFTR is a new member of the Hsp90 chaperone system, Aha1, that plays a central role in ...

In the heterozygous state, the cystic fibrosis transmembrane conductance regulator (CFTR) exon 11 mutation G551D has been described as "severe," causing pancreatic insufficiency. Two cystic fibrosis (CF) patients homozygous for this mutation showed a mild rather than severe pancreatic phenotype and a variable pulmonary phenotype.

The most prevalent form of cystic fibrosis arises from an amino acid deletion in the cystic fibrosis transmembrane conductance regulator, CFTR. A recently approved treatment for individuals homozygous for this mutation combines a chemical corrector, which helps CFTR fold, and a potentiator that increases CFTR channel activity.