ArticleThe Journal of general physiology2004
Dynamics of Ca2+-calmodulin-dependent inhibition of rod cyclic nucleotide-gated channels measured by patch-clamp fluorometry.
Article in The Journal of general physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 48 citations in OpenAlex.
- Alternative splicing governs cone cyclic nucleotide-gated (CNG) channel sensitivity to regulation by phosphoinositides.The Journal of biological chemistry · 2014Trial
- The PAS domain directly regulates hERG channel gating in patch-clamp fluorometry recordings.Biophysical journal · 2026Article
- Retinal Cyclic Nucleotide-Gated Channel Regulation by Calmodulin.International journal of molecular sciences · 2022Review
- cGMP Analogues with Opposing Actions on CNG Channels Selectively Modulate Rod or Cone Photoreceptor Function.Pharmaceutics · 2022Article
- Identification of CNGB1 as a Predictor of Response to Neoadjuvant Chemotherapy in Muscle-Invasive Bladder Cancer.Cancers · 2021Article
- A case of retinitis pigmentosa homozygous for a rare CNGA1 causal variant.Scientific reports · 2021Article
- The hERG potassium channel intrinsic ligand regulates N- and C-terminal interactions and channel closure.The Journal of general physiology · 2019Article
- hERG1a and hERG1b potassium channel subunits directly interact and preferentially form heteromeric channels.The Journal of biological chemistry · 2017Article
- Full-Spectral Multiplexing of Bioluminescence Resonance Energy Transfer in Three TRPV Channels.Biophysical journal · 2017Article
- Multiple Calmodulin-Binding Sites Positively and Negatively Regulate Arabidopsis CYCLIC NUCLEOTIDE-GATED CHANNEL12.The Plant cell · 2016Article
- Regulation of CNGA1 Channel Gating by Interactions with the Membrane.The Journal of biological chemistry · 2016Article
- The B3 Subunit of the Cone Cyclic Nucleotide-gated Channel Regulates the Light Responses of Cones and Contributes to the Channel Structural Flexibility.The Journal of biological chemistry · 2016Article
- Transition metal ion FRET to measure short-range distances at the intracellular surface of the plasma membrane.The Journal of general physiology · 2016Article
- A rendezvous with the queen of ion channels: Three decades of ion channel research by David T Yue and his Calcium Signals Laboratory.Channels (Austin, Tex.) · 2016Article
- Paul F. Cranefield award to Matthew Trudeau.The Journal of general physiology · 2015Article
- Patch-clamp fluorometry: electrophysiology meets fluorescence.Biophysical journal · 2014Review
- Calmodulin-dependent activation and inactivation of anoctamin calcium-gated chloride channels.The Journal of general physiology · 2013Article
- An IQ domain mediates the interaction with calmodulin in a plant cyclic nucleotide-gated channel.Plant & cell physiology · 2013Article
- Emerging approaches to probing ion channel structure and function.Neuroscience bulletin · 2012Review
- Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic nucleotide-gated ion channels.Nature communications · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Cyclic nucleotide-gated (CNG) ion channels mediate cellular responses to sensory stimuli. In vertebrate photoreceptors, CNG channels respond to the light-induced decrease in cGMP by closing an ion-conducting pore that is permeable to cations, including Ca(2+) ions. Rod CNG channels are directly inhibited by Ca(2+)-calmodulin (Ca(2+)/CaM), but the physiological role of this modulation is unknown. Native rod CNG channels comprise three CNGA1 subunits and one CNGB1 subunit. The single CNGB1 subunit confers several key properties on heteromeric channels, including Ca(2+)/CaM-dependent modulation. The molecular basis for Ca(2+)/CaM inhibition of rod CNG channels has been proposed to involve the binding of Ca(2+)/CaM to a site in the NH(2)-terminal region of the CNGB1 subunit, which disrupts an interaction between the NH(2)-terminal region of CNGB1 and the COOH-terminal region of CNGA1. Here, we test this mechanism for Ca(2+)/CaM-dependent inhibition of CNGA1/CNGB1 channels by simultaneously monitoring protein interactions with fluorescence spectroscopy and channel function with patch-clamp recording. Our results show that Ca(2+)/CaM binds directly to CNG channels, and that binding is the rate-limiting step for channel inhibition. Further, we show that the NH(2)- and COOH-terminal regions of CNGB1 and CNGA1 subunits, respectively, are in close proximity, and that Ca(2+)/CaM binding causes a relative rearrangement or separation of these regions. This motion occurs with the same time course as channel inhibition, consistent with the notion that rearrangement of the NH(2)- and COOH-terminal regions underlies Ca(2+)/CaM-dependent inhibition.
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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.