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Fluoride stimulates cystic fibrosis transmembrane conductance regulator Cl− channel activity
Journal article   Peer reviewed

Fluoride stimulates cystic fibrosis transmembrane conductance regulator Cl− channel activity

Herbert A Berger, Sue M Travis and Michael J Welsh
American journal of physiology. Lung cellular and molecular physiology, Vol.274(3), pp.L305-L312
03/01/1998
DOI: 10.1152/ajplung.1998.274.3.L305
PMID: 9530164

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Abstract

While studying the regulation of the cystic fibrosis transmembrane conductance regulator (CFTR), we found that addition of F− to the cytosolic surface of excised, inside-out membrane patches reversibly increased Cl− current in a dose-dependent manner. Stimulation required prior phosphorylation and the presence of ATP. F− increased current even in the presence of deferoxamine, which chelates Al3+, suggesting that stimulation was not due to A[Formula: see text]. F− also stimulated current in a CFTR variant that lacked a large part of the R domain, suggesting that the effect was not mediated via this domain. Studies of single channels showed that F−increased the open-state probability by slowing channel closure from bursts of activity; the mean closed time between bursts and single-channel conductance was not altered. These results suggested that F− influenced regulation by the cytosolic domains, most likely the nucleotide-binding domains (NBDs). Consistent with this, we found that mutation of a conserved Walker lysine in NBD2 changed the relative stimulatory effect of F− compared with wild-type CFTR, whereas mutation of the Walker lysine in NBD1 had no effect. Based on these and previous data, we speculate that F− interacts with CFTR, possibly via NBD2, and slows the rate of channel closure.

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