ArticleThe Journal of general physiology2000
A point mutation in the pore region alters gating, Ca(2+) blockage, and permeation of olfactory cyclic nucleotide-gated channels.
Article in The Journal of general physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 40 citations in OpenAlex.
- Structural mechanisms of assembly, gating, and calmodulin modulation of human olfactory CNG channel.Nature communications · 2025Article
- Mediation of mammalian olfactory response by presence of odor-evoked potassium current.Frontiers in allergy · 2024Article
- CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021Review
- Article
- Structural implications of weak Ca2+ block in Drosophila cyclic nucleotide-gated channels.The Journal of general physiology · 2015Article
- Article
- Normal-mode-analysis-guided investigation of crucial intersubunit contacts in the cAMP-dependent gating in HCN channels.Biophysical journal · 2012Article
- Structural studies of ion selectivity in tetrameric cation channels.The Journal of general physiology · 2011Review
- Structural studies of ion permeation and Ca2+ blockage of a bacterial channel mimicking the cyclic nucleotide-gated channel pore.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Gating at the selectivity filter in cyclic nucleotide-gated channels.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Structural insight into Ca2+ specificity in tetrameric cation channels.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Access of quaternary ammonium blockers to the internal pore of cyclic nucleotide-gated channels: implications for the location of the gate.The Journal of general physiology · 2006Article
- A single P-loop glutamate point mutation to either lysine or arginine switches the cation-anion selectivity of the CNGA2 channel.The Journal of general physiology · 2006Article
- Mutation of the pore glutamate affects both cytoplasmic and external dequalinium block in the rat olfactory CNGA2 channel.European biophysics journal : EBJ · 2005Article
- Molecular basis of an inherited form of incomplete achromatopsia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004Article
- Gating of heteromeric retinal rod channels by cyclic AMP: role of the C-terminal and pore domains.Biophysical journal · 2002Article
- Cyclic nucleotide-gated channels: shedding light on the opening of a channel pore.Nature reviews. Neuroscience · 2001Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Upon stimulation by odorants, Ca(2+) and Na(+) enter the cilia of olfactory sensory neurons through channels directly gated by cAMP. Cyclic nucleotide-gated channels have been found in a variety of cells and extensively investigated in the past few years. Glutamate residues at position 363 of the alpha subunit of the bovine retinal rod channel have previously been shown to constitute a cation-binding site important for blockage by external divalent cations and to control single-channel properties. It has therefore been assumed, but not proven, that glutamate residues at the corresponding position of the other cyclic nucleotide-gated channels play a similar role. We studied the corresponding glutamate (E340) of the alpha subunit of the bovine olfactory channel to determine its role in channel gating and in permeation and blockage by Ca(2+) and Mg(2+). E340 was mutated into either an aspartate, glycine, glutamine, or asparagine residue and properties of mutant channels expressed in Xenopus laevis oocytes were measured in excised patches. By single-channel recordings, we demonstrated that the open probabilities in the presence of cGMP or cAMP were decreased by the mutations, with a larger decrease observed on gating by cAMP. Moreover, we observed that the mutant E340N presented two conductance levels. We found that both external Ca(2+) and Mg(2+) powerfully blocked the current in wild-type and E340D mutants, whereas their blockage efficacy was drastically reduced when the glutamate charge was neutralized. The inward current carried by external Ca(2+) relative to Na(+) was larger in the E340G mutant compared with wild-type channels. In conclusion, we have confirmed that the residue at position E340 of the bovine olfactory CNG channel is in the pore region, controls permeation and blockage by external Ca(2+) and Mg(2+), and affects channel gating by cAMP more than by cGMP.
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