ArticleCell research2016
Structural insights into Ca(2+)-activated long-range allosteric channel gating of RyR1.
Article in Cell research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Correlation of phenotype with genotype and protein structure in RYR1-related disorders.Journal of neurology · 2018Trial
- Cylindrical Crystallization of CaInternational journal of molecular sciences · 2026Review
- Structural and Functional Regulation of RyR2 in Cardiac Calcium Handling and Arrhythmogenesis.Biomedicines · 2026Review
- A Model Framework for Ion Channels with Selectivity Filters Based on Non-Equilibrium Thermodynamics.Entropy (Basel, Switzerland) · 2025Article
- Structure-based mechanism of RyR channel operation by calcium and magnesium ions.PLoS computational biology · 2025Article
- Structural insights into transmembrane helix S0 facilitated RyR1 channel gating by CaNature communications · 2025Article
- In situ structural insights into the excitation-contraction coupling mechanism of skeletal muscle.Science advances · 2024Article
- Molecular basis for gating of cardiac ryanodine receptor explains the mechanisms for gain- and loss-of function mutations.Nature communications · 2022Article
- Structural basis for activation and gating of IPNature communications · 2022Article
- Programmable allosteric DNA regulations for molecular networks and nanomachines.Science advances · 2022Article
- Mapping co-regulatory interactions among ligand-binding sites in ryanodine receptor 1.Proteins · 2022Article
- High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor.Structure (London, England : 1993) · 2022Article
- Structural Insight Into Ryanodine Receptor Channelopathies.Frontiers in pharmacology · 2022Review
- Identification of Potential Human Ryanodine Receptor 1 Agonists and Molecular Mechanisms of Natural Small-Molecule Phenols as Anxiolytics.ACS omega · 2021Article
- Regulatory mechanisms of ryanodine receptor/CaJournal of muscle research and cell motility · 2021Review
- Identification of an amino-terminus determinant critical for ryanodine receptor/Ca2+ release channel function.Cardiovascular research · 2021Article
- Status and outlook for acaricide and insecticide discovery.Pest management science · 2021Review
- Intracellular calcium leak in heart failure and atrial fibrillation: a unifying mechanism and therapeutic target.Nature reviews. Cardiology · 2020Review
- Retrieving functional pathways of biomolecules from single-particle snapshots.Nature communications · 2020Article
- Structure and Function of the Human Ryanodine Receptors and Their Association with Myopathies-Present State, Challenges, and Perspectives.Molecules (Basel, Switzerland) · 2020Review
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16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ryanodine receptors (RyRs) are a class of giant ion channels with molecular mass over 2.2 mega-Daltons. These channels mediate calcium signaling in a variety of cells. Since more than 80% of the RyR protein is folded into the cytoplasmic assembly and the remaining residues form the transmembrane domain, it has been hypothesized that the activation and regulation of RyR channels occur through an as yet uncharacterized long-range allosteric mechanism. Here we report the characterization of a Ca(2+)-activated open-state RyR1 structure by cryo-electron microscopy. The structure has an overall resolution of 4.9 Å and a resolution of 4.2 Å for the core region. In comparison with the previously determined apo/closed-state structure, we observed long-range allosteric gating of the channel upon Ca(2+) activation. In-depth structural analyses elucidated a novel channel-gating mechanism and a novel ion selectivity mechanism of RyR1. Our work not only provides structural insights into the molecular mechanisms of channel gating and regulation of RyRs, but also sheds light on structural basis for channel-gating and ion selectivity mechanisms for the six-transmembrane-helix cation channel family.
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