Related Experiment Video
Updated: May 2, 2026

Expression and Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein in Saccharomyces cerevisiae
Published on: March 10, 2012
CFTR: new members join the fold
1Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, OR 97239, USA. skachw@ohsu.edu
Abstract:
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 CFTR folding.
More Related Videos
Related Concept Videos
ABC Transporters: Importer
In bacteria, based on the number of transmembrane helices and the chemical nature of their substrates, the ABC importers can be divided into three types:
Cotranslational Protein Translocation
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Insertion of Single-pass Transmembrane Proteins in the RER
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Total Internal Reflection Fluorescence Microscopy
Cystic Fibrosis: Pathogenesis
CF is primarily caused by a genetic mutation in a chromosome 7 gene coding for the cystic fibrosis transmembrane conductance regulator (CFTR) protein. The most common gene mutation leading to CF is the ΔF508 mutation,...
Cystic Fibrosis: Management
Sinus disease and chronic...

