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Correctors of mutant CFTR enhance subcortical cAMP-PKA signaling through modulating ezrin phosphorylation and cytoskeleton organization.

J Cell Sci. 2016; 
Abbattiscianni AC, Favia M, Mancini MT, Cardone RA, Guerra L, Monterisi S, Castellani S, Laselva O, Di Sole F, Conese M, Zaccolo M, Casavola V.
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Polyclonal Antibody Services Louis, MO), polyclonal anti-Ezrin (GenScript, Piscataway, USA), polyclonal anti-human NHERF1 (Thermo Fisher Scientific Inc. Get A Quote

摘要

The most common mutation of the cystic fibrosis transmembrane regulator (CFTR) gene, F508del, produces a misfolded protein resulting in its defective trafficking to the cell surface and an impaired chloride secretion. Pharmacological treatments partially rescue F508del CFTR activity either directly by interacting with the mutant protein and/or indirectly by altering the cellular protein homeostasis. Here, we show that the phosphorylation of ezrin together with its binding to phosphatidylinositol-4,5-bisphosphate (PIP2) tethers the F508del CFTR to the actin cytoskeleton, stabilizing it on the apical membrane and rescuing the sub-membrane compartmentalization of cAMP and activated PKA. Both the small molecules tr... More

關鍵詞

Airway cells; Correctors; Cystic fibrosis; FRET; PKA; cAMP
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