Journal
CHANNELS
Volume 9, Issue 2, Pages 88-95Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/19336950.2015.1027849
Keywords
calcium-activated chloride channels; ion permeation; pore; pore blockers; TMEM16A; Xenopus tropicalis A-9-C; anthracene-9-carboxylic acid; DIDS; 4,4 '-Diisothiocyano-2,2 '-stilbenedisulfonic acid
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Funding
- PAPIIT [IN200913, IA201413]
- CONACyT [220224]
- CONACyT
- Posgrado en Ciencias Biomedicas-UNAM
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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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