ArticleBiochemistry2014
Two regions of the ryanodine receptor calcium channel are involved in Ca(2+)-dependent inactivation.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 38 citations in OpenAlex.
- Characterization of cardiac disease-associated mutations in RyR2 CaAmerican journal of physiology. Cell physiology · 2026Article
- Cryo-EM Brings the Mechanisms of Activation, Inactivation, and Inhibition of Ryanodine Receptors into Focus.Advances in experimental medicine and biology · 2026Review
- Modeling traveling calcium waves in cellular structures.Journal of computational neuroscience · 2025Article
- Structure-based mechanism of RyR channel operation by calcium and magnesium ions.PLoS computational biology · 2025Article
- The biophysical properties of TRIC-A and TRIC-B and their interactions with RyR2.The Journal of general physiology · 2023Article
- CaeLife · 2022Article
- Structural Insight Into Ryanodine Receptor Channelopathies.Frontiers in pharmacology · 2022Review
- Regulatory mechanisms of ryanodine receptor/CaJournal of muscle research and cell motility · 2021Review
- Structure and function of the calcium-selective TRP channel TRPV6.The Journal of physiology · 2021Review
- Retrieving functional pathways of biomolecules from single-particle snapshots.Nature communications · 2020Article
- CaCell calcium · 2020Review
- CaThe Journal of biological chemistry · 2018Article
- Mechanism of calmodulin inactivation of the calcium-selective TRP channel TRPV6.Science advances · 2018Article
- Single-channel recordings of RyR1 at microsecond resolution in CMOS-suspended membranes.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- G4941K substitution in the pore-lining S6 helix of the skeletal muscle ryanodine receptor increases RyR1 sensitivity to cytosolic and luminal CaThe Journal of biological chemistry · 2018Article
- Ryanodine Receptor Structure and Function in Health and Disease.Sub-cellular biochemistry · 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
- Lanthanides Report Calcium Sensor in the Vestibule of Ryanodine Receptor.Biophysical journal · 2017Article
- Extensive Ca2+ leak through K4750Q cardiac ryanodine receptors caused by cytosolic and luminal Ca2+ hypersensitivity.The Journal of general physiology · 2017Article
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2 authors at 2 institutions in 1 country.
Funding
Abstract
Skeletal (RyR1) and cardiac muscle (RyR2) isoforms of ryanodine receptor calcium channels are inhibited by millimollar Ca(2+), but the affinity of RyR2 for inhibitory Ca(2+) is ~10 times lower than that of RyR1. Previous studies demonstrated that the C-terminal quarter of RyR has critical domain(s) for Ca(2+) inactivation. To obtain further insights into the molecular basis of regulation of RyRs by Ca(2+), we constructed and expressed 18 RyR1-RyR2 chimeras in HEK293 cells and determined the Ca(2+) activation and inactivation affinities of these channels using the [(3)H]ryanodine binding assay. Replacing two distinct regions of RyR1 with corresponding RyR2 sequences reduced the affinity for Ca(2+) inactivation. The first region (RyR2 amino acids 4020-4250) contains two EF-hand Ca(2+) binding motifs (EF1, amino acids 4036-4047; EF2, amino acids 4071-4082), and the second region includes the putative second transmembrane segment (S2). A RyR1-backbone chimera containing only EF2 from RyR2 had a modest (not significant) change in Ca(2+) inactivation, whereas another chimera channel carrying only EF1 from RyR2 had a significantly reduced level of Ca(2+) inactivation. The results suggest that EF1 is a more critical determinant for RyR inactivation by Ca(2+). In addition, activities of the chimera carrying RyR2 EF-hands were suppressed at 10-100 μM Ca(2+), and the suppression was relieved by 1 mM Mg(2+). The same effects have been observed with wild-type RyR2. A mutant RyR1 carrying both regions replaced with RyR2 sequences (amino acids 4020-4250 and 4560-4618) showed a Ca(2+) inactivation affinity comparable to that of RyR2, indicating that these regions are sufficient to confer RyR2-type Ca(2+)-dependent inactivation on RyR1.
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