ArticleProceedings of the National Academy of Sciences of the United States of America2002
Mechanism of calcium/calmodulin inhibition of rod cyclic nucleotide-gated channels.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 72 citations in OpenAlex.
- Alternative splicing governs cone cyclic nucleotide-gated (CNG) channel sensitivity to regulation by phosphoinositides.The Journal of biological chemistry · 2014Trial
- Structural mechanisms of assembly, gating, and calmodulin modulation of human olfactory CNG channel.Nature communications · 2025Article
- Retained introns in phototransduction genes of 5xFAD mouse retina suggest vision impairment as an early diagnostic marker for Alzheimer's disease.Scientific reports · 2025Article
- Genome-wide identification of cyclic nucleotide-gated channel gene family inFrontiers in plant science · 2025Article
- Feedforward and feedback mechanisms cooperatively regulate rapid experience-dependent response adaptation in a single thermosensory neuron type.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Feedforward and feedback mechanisms cooperatively regulate rapid experience-dependent response adaptation in a single thermosensory neuron type.bioRxiv : the preprint server for biology · 2023Article
- Retinal Cyclic Nucleotide-Gated Channel Regulation by Calmodulin.International journal of molecular sciences · 2022Review
- Chemical shift assignments of calmodulin bound to a C-terminal site (residues 1120-1147) in the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1).Biomolecular NMR assignments · 2022Article
- NMR Structures of Calmodulin Bound to Two Separate Regulatory Sites in the Retinal Cyclic Nucleotide-Gated Channel.Biochemistry · 2022Article
- Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1).Biomolecular NMR assignments · 2022Article
- Pangenome-wide analysis of cyclic nucleotide-gated channel (CNGC) gene family in citrusFrontiers in genetics · 2022Article
- Deciphering the Role of Ion Channels in Early Defense Signaling against Herbivorous Insects.Cells · 2021Review
- Article
- Multiple Calmodulin-Binding Sites Positively and Negatively Regulate Arabidopsis CYCLIC NUCLEOTIDE-GATED CHANNEL12.The Plant cell · 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
- Interactions between N and C termini of α1C subunit regulate inactivation of CaV1.2 L-type Ca(2+) channel.Channels (Austin, Tex.) · 2016Article
- Inherited macular degeneration-associated mutations in CNGB3 increase the ligand sensitivity and spontaneous open probability of cone cyclic nucleotide-gated channels.Frontiers in physiology · 2015Article
- Paul F. Cranefield award to Matthew Trudeau.The Journal of general physiology · 2015Article
- Article
- CNGA3 achromatopsia-associated mutation potentiates the phosphoinositide sensitivity of cone photoreceptor CNG channels by altering intersubunit interactions.American journal of physiology. Cell physiology · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Rod cyclic nucleotide-gated (CNG) channels are heterotetramers comprised of both CNGA1 and CNGB1 subunits. Calcium/calmodulin (Ca(2+)/CaM) binds to a site in the N-terminal region of CNGB1 subunits and inhibits the opening conformational change in CNGA1/CNGB1 channels. Here, we show that polypeptides derived from an N-terminal region of CNGB1 form a specific interaction with polypeptides derived from a C-terminal region of CNGA1 that is distal to the cyclic nucleotide-binding domain. Deletion of the Ca(2+)/CaM-binding site from the N-terminal region of CNGB1 eliminated both Ca(2+)/CaM modulation of the channel and the intersubunit interaction. Furthermore, the interaction was disrupted by the presence of Ca(2+)/CaM. These results suggest that Ca(2+)/CaM-dependent inhibition of rod channels is caused by the direct binding of Ca(2+)/CaM to a site in the N-terminal region in CNGB1, which disrupts the interaction between this region and a distal C-terminal region of CNGA1. The mechanism underlying Ca(2+)/CaM modulation of rod channels is distinct from that in olfactory (CNGA2) CNG channels.
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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.