Macrocycle-stabilization of its interaction with 14-3-3 increases plasma membrane localization and activity of CFTR View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2022-06-23

AUTHORS

Loes M. Stevers, Madita Wolter, Graeme W. Carlile, Dwight Macdonald, Luc Richard, Frank Gielkens, John W. Hanrahan, David Y. Thomas, Sai Kumar Chakka, Mark L. Peterson, Helmut Thomas, Luc Brunsveld, Christian Ottmann

ABSTRACT

Impaired activity of the chloride channel CFTR is the cause of cystic fibrosis. 14-3-3 proteins have been shown to stabilize CFTR and increase its biogenesis and activity. Here, we report the identification and mechanism of action of a macrocycle stabilizing the 14-3-3/CFTR complex. This molecule rescues plasma membrane localization and chloride transport of F508del-CFTR and works additively with the CFTR pharmacological chaperone corrector lumacaftor (VX-809) and the triple combination Trikafta®. This macrocycle is a useful tool to study the CFTR/14-3-3 interaction and the potential of molecular glues in cystic fibrosis therapeutics. More... »

PAGES

3586

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-022-31206-6

DOI

http://dx.doi.org/10.1038/s41467-022-31206-6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1148899286

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/35739107


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