ArticleBiophysical journal2006
Gating of cyclic nucleotide-gated (CNGA1) channels by cGMP jumps and depolarizing voltage steps.
Article in Biophysical journal, 2006. 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, 17 citations in OpenAlex.
- PIP2 binding at allosteric site blocks activation in human rod CNG channels.Nature communications · 2026Article
- Selectivity Filter Dynamics Define Ion Conductance and Selectivity Differences in CNG and HCN Channels.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Reverse Engineering Caged Compounds: Design Principles for their Application in Biology.Angewandte Chemie (International ed. in English) · 2023Review
- Subunit promotion energies for channel opening in heterotetrameric olfactory CNG channels.PLoS computational biology · 2022Article
- CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021Review
- Article
- Ligand binding and activation properties of the purified bacterial cyclic nucleotide-gated channel SthK.The Journal of general physiology · 2018Article
- Proton transfer unlocks inactivation in cyclic nucleotide-gated A1 channels.The Journal of physiology · 2015Article
- Multiple mechanisms underlying rectification in retinal cyclic nucleotide-gated (CNGA1) channels.Physiological reports · 2013Article
- Mutations reveal voltage gating of CNGA1 channels in saturating cGMP.The Journal of general physiology · 2009Article
- The structure of the prokaryotic cyclic nucleotide-modulated potassium channel MloK1 at 16 A resolution.Structure (London, England : 1993) · 2007Article
Corrections and comments
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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
We expressed rod-type homotetrameric cyclic nucleotide-gated (CNGA1) channels in Xenopus oocytes and studied activation by photolysis-induced jumps of the 3',5'-cyclic guanosine monophosphate (cGMP) concentration and by voltage steps. cGMP jumps to increasing concentrations up to the EC50 value of 46.5 microM decelerate the activation gating, indicative that even at concentrations of cGMP << EC50 binding is not rate limiting. Above the EC50 value, activation by cGMP jumps is again accelerated to the higher concentrations. At the same cGMP concentration, the speed of the activation gating by depolarizing voltage steps is roughly similar to that by cGMP jumps. Permeating ions passing the pore more slowly (Rb+ > K+ > Na+) slow down the activation time course. At the single-channel level, cGMP jumps to high concentrations cause openings directly to the main open level without passing sublevels. From these results it is concluded that at both low and high cGMP the gating of homotetrameric CNGA1 channels is not rate-limited by the cGMP binding but by conformational changes of the channel which are voltage dependent and include movements in the pore region.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.