ArticleThe EMBO journal1999
Molecular determinants of a Ca2+-binding site in the pore of cyclic nucleotide-gated channels: S5/S6 segments control affinity of intrapore glutamates.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 73 citations in OpenAlex.
- Structural basis of properties, mechanisms, and channelopathy of cyclic nucleotide-gated channels.Channels (Austin, Tex.) · 2023Review
- Structural basis of calmodulin modulation of the rod cyclic nucleotide-gated channel.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Gating intermediates reveal inhibitory role of the voltage sensor in a cyclic nucleotide-modulated ion channel.Nature communications · 2022Article
- The structure of the native CNGA1/CNGB1 CNG channel from bovine retinal rods.Nature structural & molecular biology · 2022Article
- Article
- Chemosensory signal transduction in Caenorhabditis elegans.Genetics · 2021Review
- Function and regulation of TRPP2 ion channel revealed by a gain-of-function mutant.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Proton transfer unlocks inactivation in cyclic nucleotide-gated A1 channels.The Journal of physiology · 2015Article
- Cell- and subunit-specific mechanisms of CNG channel ciliary trafficking and localization in C. elegans.Journal of cell science · 2013Article
- CNGA3 is expressed in inner ear hair cells and binds to an intracellular C-terminus domain of EMILIN1.The Biochemical journal · 2012Article
- Mechanism for modulation of gating of connexin26-containing channels by taurine.The Journal of general physiology · 2011Article
- 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
- Functional equivalency inferred from "authoritative sources" in networks of homologous proteins.PloS one · 2009Article
- Structural insight into Ca2+ specificity in tetrameric cation channels.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Ca2+-dependent inactivation of CaV1.2 channels prevents Gd3+ block: does Ca2+ block the pore of inactivated channels?The Journal of general physiology · 2007Article
- Acidic amino acids impart enhanced Ca2+ permeability and flux in two members of the ATP-gated P2X receptor family.The Journal of general physiology · 2007Article
- Open channel block by Ca2+ underlies the voltage dependence of drosophila TRPL channel.The Journal of general physiology · 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
- The pharmacology of cyclic nucleotide-gated channels: emerging from the darkness.Current pharmaceutical design · 2006Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyclic nucleotide-gated (CNG) channels play an important role in Ca2+ signaling in many cells. CNG channels from various tissues differ profoundly in their Ca2+ permeation properties. Using the voltage-dependent Ca2+ blockage of monovalent current in wild-type channels, chimeric constructs and point mutants, we have identified structural elements that determine the distinctively different interaction of Ca2+ with CNG channels from rod and cone photoreceptors and olfactory neurons. Segments S5 and S6 and the extracellular linkers flanking the pore region are the only structural elements that account for the differences between channels. Ca2+ blockage is strongly modulated by external pH. The different pH dependence of blockage suggests that the pKa of intrapore glutamates and their protonation pattern differ among channels. The results support the hypothesis that the S5-pore-S6 module, by providing a characteristic electrostatic environment, determines the protonation state of pore glutamates and thereby controls Ca2+ affinity and permeation in each channel type.
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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.