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XB-ART-50325
Channels (Austin) 2015 Jan 01;92:88-95. doi: 10.1080/19336950.2015.1027849.
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Study of permeation and blocker binding in TMEM16A calcium-activated chloride channels.

Reyes JP , Huanosta-Gutiérrez A , López-Rodríguez A , Martínez-Torres A .


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We studied the effects of mutations of positively charged amino acid residues in the pore of X. tropicalis TMEM16A calcium-activated chloride channels: K613E, K628E, K630E; R646E and R761E. The activation and deactivation kinetics were not affected, and only K613E showed a lower current density. K628E and R761E affect anion selectivity without affecting Na(+) permeation, whereas K613E, R646E and the double mutant K613E + R646E affect anion selectivity and permeability to Na(+). Furthermore, altered blockade by the chloride channel blockers anthracene-9-carboxylic acid (A-9-C), 4, 4'-Diisothiocyano-2,2'-stilbenedisulfonic acid (DIDS) and T16inh-A01 was observed. These results suggest the existence of 2 binding sites for anions within the pore at electrical distances of 0.3 and 0.5. These sites are also relevant for anion permeation and blockade.

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Species referenced: Xenopus tropicalis
Genes referenced: ano1

References [+] :
Betto, Interactions between permeation and gating in the TMEM16B/anoctamin2 calcium-activated chloride channel. 2014, Pubmed