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Study of permeation and blocker binding in TMEM16A calcium-activated chloride channels.


ABSTRACT: 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.

SUBMITTER: Reyes JP 

PROVIDER: S-EPMC4594575 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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Study of permeation and blocker binding in TMEM16A calcium-activated chloride channels.

Reyes J P JP   Huanosta-Gutiérrez A A   López-Rodríguez A A   Martínez-Torres A A  

Channels (Austin, Tex.) 20150101 2


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, alte  ...[more]

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