ArticlePhysiological reports2013
Multiple mechanisms underlying rectification in retinal cyclic nucleotide-gated (CNGA1) channels.
Article in Physiological reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 11 citations in OpenAlex.
- Structural basis of properties, mechanisms, and channelopathy of cyclic nucleotide-gated channels.Channels (Austin, Tex.) · 2023Review
- Article
- Mechanism Study of Proteins under Membrane Environment.Membranes · 2022Article
- Mathematical Modeling of Monovalent Permselectivity of a Bilayer Ion-Exchange Membrane as a Function of Current Density.International journal of molecular sciences · 2022Article
- Simulation atomic force microscopy for atomic reconstruction of biomolecular structures from resolution-limited experimental images.PLoS computational biology · 2022Article
- CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021Review
- The permeation mechanism of organic cations through a CNG mimic channel.PLoS computational biology · 2018Article
- The gating mechanism in cyclic nucleotide-gated ion channels.Scientific reports · 2018Article
- Article
- Structural Heterogeneity of CNGA1 Channels Revealed by Electrophysiology and Single-Molecule Force Spectroscopy.ACS omega · 2016Article
- A structural, functional, and computational analysis suggests pore flexibility as the base for the poor selectivity of CNG channels.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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 dimethylammonium shows that at least two voltage-dependent transitions underlie the observed rectification. Only the first voltage-dependent transition is sensible to mutation of charge residues in the S4 helix. Moreover, analysis of tail and gating currents indicates that the number of elementary charges per channel moving across the membrane is less than 2, when they are about 12 in K(+) channels. These results indicate the existence of distinct mechanisms underlying rectification in CNG channels. A restricted motion of the S4 helix together with an inefficient coupling to the channel gate render CNGA1 channels poorly sensitive to voltage in the presence of physiological Na(+) and K(+).
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