Rescuing A Cystic Fibrosis Protein | Chemical & Engineering News
Volume 93 Issue 48 | p. 36 | Concentrates
Issue Date: December 7, 2015

Rescuing A Cystic Fibrosis Protein

Proteomics: Changes in protein interactions restore function of a mutant ion channel involved in the debilitating disease
Department: Science & Technology
News Channels: Analytical SCENE, Biological SCENE
Keywords: cystic fibrosis, interactomes, mass spectrometry, protein interactions

The most common cause of cystic fibrosis is a mutation in which a missing phenylalanine leads to an almost complete loss of function of the cystic fibrosis transmembrane conductance regulator (CFTR). This ion channel protein is involved in maintaining salt balance in the lungs and other tissues. CFTR’s function can be partially restored by incubating cells at lower temperatures or inhibiting histone deacetylase enzymes. But how these rescue approaches affect CFTR’s protein interaction network, or interactome, isn’t known. To find out, Sandra Pankow, John R. Yates III, and coworkers at Scripps Research Institute California used immunocoprecipitation and mass spectrometry of cultured human bronchial cells to identify the interactomes for normal and mutated CFTR under normal and rescue conditions (Nature 2015, DOI: 10.1038/nature15729). By comparing how the interaction networks change in response to the rescue strategies, the researchers identified pathways that enable CFTR rescue. Although rescue strategies eliminate most mutant-specific interactions, seven interactions involving protein-degradation machinery persist in both approaches, suggesting that even under rescue conditions mutant CFTR is fated for degradation.

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ISSN 0009-2347
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