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...

Malfunction of cystic fibrosis transmembrane conductance regulator (CFTR), a member of the ABC protein superfamily that functions as an ATP-gated chloride channel, causes the lethal genetic disease, cystic fibrosis. This review focuses on the most recent findings on the gating mechanism of CFTR. Potential clinical relevance and implications to ABC transporter function are also discussed.

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 ...