ArticleThe Journal of biological chemistry2012
Calmodulin-binding locations on the skeletal and cardiac ryanodine receptors.
Article in The Journal of biological chemistry, 2012. 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.
- In situ structural insights into the excitation-contraction coupling mechanism of skeletal muscle.Science advances · 2024Article
- Structural Insight Into Ryanodine Receptor Channelopathies.Frontiers in pharmacology · 2022Review
- Resolved Structural States of Calmodulin in Regulation of Skeletal Muscle Calcium Release.Biophysical journal · 2020Article
- Statin-Related Myotoxicity: A Comprehensive Review of Pharmacokinetic, Pharmacogenomic and Muscle Components.Journal of clinical medicine · 2019Review
- Article
- CaThe Biochemical journal · 2019Article
- Calmodulinopathy: Functional Effects of CALM Mutations and Their Relationship With Clinical Phenotypes.Frontiers in cardiovascular medicine · 2018Review
- The structural basis of ryanodine receptor ion channel function.The Journal of general physiology · 2017Review
- Two EF-hand motifs in ryanodine receptor calcium release channels contribute to isoform-specific regulation by calmodulin.Cell calcium · 2017Article
- A guide to the 3D structure of the ryanodine receptor type 1 by cryoEM.Protein science : a publication of the Protein Society · 2017Review
- Review of RyR1 pathway and associated pathomechanisms.Acta neuropathologica communications · 2016Review
- S100A1 Protein Does Not Compete with Calmodulin for Ryanodine Receptor Binding but Structurally Alters the Ryanodine Receptor·Calmodulin Complex.The Journal of biological chemistry · 2016Article
- A local-optimization refinement algorithm in single particle analysis for macromolecular complex with multiple rigid modules.Protein & cell · 2016Article
- Arrhythmogenic Calmodulin Mutations Affect the Activation and Termination of Cardiac Ryanodine Receptor-mediated Ca2+ Release.The Journal of biological chemistry · 2015Article
- Article
- FRET-based trilateration of probes bound within functional ryanodine receptors.Biophysical journal · 2014Article
- Cardiac myocyte Z-line calmodulin is mainly RyR2-bound, and reduction is arrhythmogenic and occurs in heart failure.Circulation research · 2014Article
- Two potential calmodulin-binding sequences in the ryanodine receptor contribute to a mobile, intra-subunit calmodulin-binding domain.Journal of cell science · 2013Article
- Allosteric mechanism of water-channel gating by Ca2+-calmodulin.Nature structural & molecular biology · 2013Article
- Deformed grids for single-particle cryo-electron microscopy of specimens exhibiting a preferred orientation.Journal of structural biology · 2013Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Ryanodine receptor types 1 (RyR1) and 2 (RyR2) are calcium release channels that are highly enriched in skeletal and cardiac muscle, respectively, where they play an essential role in excitation-contraction coupling. Apocalmodulin (apo-CaM) weakly activates RyR1 but inhibits RyR2, whereas Ca(2+)-calmodulin inhibits both isoforms. Previous cryo-EM studies showed distinctly different binding locations on RyR1 for the two states of CaM. However, recent studies employing FRET appear to challenge these findings. Here, using cryo-EM, we have determined that a CaM mutant that is incapable of binding calcium binds to RyR1 at the apo site, regardless of the calcium concentration. We have also re-determined the location of RyR1-bound Ca(2+)-CaM using uniform experimental conditions. Our results show the existence of the two overlapping but distinct binding sites for CaM in RyR1 and imply that the binding location switch is due to Ca(2+) binding to CaM, as opposed to direct effects of Ca(2+) on RyR1. We also discuss explanations that could resolve the apparent conflict between the cryo-EM and FRET results. Interestingly, apo-CaM binds to RyR2 at a similar binding location to that of Ca(2+)-CaM on RyR1, in seeming agreement with the inhibitory effects of these two forms of CaM on their respective receptors.
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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.