ArticleThe Journal of biological chemistry2016
The EF-hand Ca2+ Binding Domain Is Not Required for Cytosolic Ca2+ Activation of the Cardiac Ryanodine Receptor.
Article in The Journal of biological chemistry, 2016. 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, 43 citations in OpenAlex.
- Review
- Non-ionotropic voltage-gated calcium channel signaling.Channels (Austin, Tex.) · 2024Review
- CCAR-1 works together with the U2AF large subunit UAF-1 to regulate alternative splicing.RNA biology · 2024Article
- Functional determination of calcium-binding sites required for the activation of inositol 1,4,5-trisphosphate receptors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A Comparative Perspective on Functionally-Related, Intracellular Calcium Channels: The Insect Ryanodine and Inositol 1,4,5-Trisphosphate Receptors.Biomolecules · 2021Review
- Identification of loss-of-function RyR2 mutations associated with idiopathic ventricular fibrillation and sudden death.Bioscience reports · 2021Article
- Disrupting polycystin-2 EF hand CaJournal of cell science · 2020Article
- The central domain of cardiac ryanodine receptor governs channel activation, regulation, and stability.The Journal of biological chemistry · 2020Article
- Retrieving functional pathways of biomolecules from single-particle snapshots.Nature communications · 2020Article
- Structure and Function of IPCold Spring Harbor perspectives in biology · 2019Review
- Ryanodine Receptor Structure and Function in Health and Disease.Sub-cellular biochemistry · 2018Review
- 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
- Control of cardiac ryanodine receptor by sarcoplasmic reticulum luminal CaThe 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
- CaTrends in biochemical sciences · 2017Review
- Intracellular CaMolecular cell · 2017Review
- Lanthanides Report Calcium Sensor in the Vestibule of Ryanodine Receptor.Biophysical journal · 2017Article
- The Cytoplasmic Region of Inner Helix S6 Is an Important Determinant of Cardiac Ryanodine Receptor Channel Gating.The Journal of biological chemistry · 2016Article
- Malignant hyperthermia-associated mutations in the S2-S3 cytoplasmic loop of type 1 ryanodine receptor calcium channel impair calcium-dependent inactivation.American journal of physiology. Cell physiology · 2016Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Activation of the cardiac ryanodine receptor (RyR2) by elevating cytosolic Ca(2+) is a central step in the process of Ca(2+)-induced Ca(2+) release, but the molecular basis of RyR2 activation by cytosolic Ca(2+) is poorly defined. It has been proposed recently that the putative Ca(2+) binding domain encompassing a pair of EF-hand motifs (EF1 and EF2) in the skeletal muscle ryanodine receptor (RyR1) functions as a Ca(2+) sensor that regulates the gating of RyR1. Although the role of the EF-hand domain in RyR1 function has been studied extensively, little is known about the functional significance of the corresponding EF-hand domain in RyR2. Here we investigate the effect of mutations in the EF-hand motifs on the Ca(2+) activation of RyR2. We found that mutations in the EF-hand motifs or deletion of the entire EF-hand domain did not affect the Ca(2+)-dependent activation of [(3)H]ryanodine binding or the cytosolic Ca(2+) activation of RyR2. On the other hand, deletion of the EF-hand domain markedly suppressed the luminal Ca(2+) activation of RyR2 and spontaneous Ca(2+) release in HEK293 cells during store Ca(2+) overload or store overload-induced Ca(2+) release (SOICR). Furthermore, mutations in the EF2 motif, but not EF1 motif, of RyR2 raised the threshold for SOICR termination, whereas deletion of the EF-hand domain of RyR2 increased both the activation and termination thresholds for SOICR. These results indicate that, although the EF-hand domain is not required for RyR2 activation by cytosolic Ca(2+), it plays an important role in luminal Ca(2+) activation and SOICR.
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