Multiple mechanisms underlying rectification in retinal cyclic nucleotide-gated (CNGA1) channels.

ABSTRACT: In cyclic nucleotide-gated (CNGA1) channels, in the presence of symmetrical ionic conditions, current-voltage (I-V) relationship depends, in a complex way, on the radius of permeating ion. It has been suggested that both the pore and S4 helix contribute to the observed rectification. In the present manuscript, using tail and gating current measurements from homotetrameric CNGA1 channels expressed in Xenopus oocytes, we clarify and quantify the role of the pore and of the S4 helix. We show that in symmetrical Rb(+) and Cs(+) single-channel current rectification dominates macroscopic currents while voltage-dependent gating becomes larger in symmetrical ethylammonium and dimethylammonium, where the open probability strongly depends on voltage. Isochronal tail currents analysis in dimethylammo

SUBMITTER: Arcangeletti M 

PROVIDER: S-EPMC3871463 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature