ArticleBiophysical journal2006
A Ca2+-binding domain in RyR1 that interacts with the calmodulin binding site and modulates channel activity.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.
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Who cites it
28 citing papers in PubMed, 1 synthesis or guideline pooled it, 69 citations in OpenAlex.
- An Updated Meta-Analysis Based on the Preclinical Evidence of Mechanism of Aconitine-Induced Cardiotoxicity.Frontiers in pharmacology · 2022Pooled it
- Prenatal diagnosis identifies compound heterozygous variants in RYR1 that causes ultrasound abnormalities in a fetus.BMC medical genomics · 2022Article
- CaFrontiers in cellular neuroscience · 2022Review
- RyR1-related myopathy mutations in ATP and calcium binding sites impair channel regulation.Acta neuropathologica communications · 2021Article
- Mechanistic link between CaM-RyR2 interactions and the genesis of cardiac arrhythmia.Biophysical journal · 2021Article
- The Calcium Signaling Mechanisms in Arterial Smooth Muscle and Endothelial Cells.Comprehensive Physiology · 2021Article
- Intracellular calcium leak in heart failure and atrial fibrillation: a unifying mechanism and therapeutic target.Nature reviews. Cardiology · 2020Review
- 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
- 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
- Article
- The EF-hand Ca2+ Binding Domain Is Not Required for Cytosolic Ca2+ Activation of the Cardiac Ryanodine Receptor.The Journal of biological chemistry · 2016Article
- Structure of a mammalian ryanodine receptor.Nature · 2015Article
- Two regions of the ryanodine receptor calcium channel are involved in Ca(2+)-dependent inactivation.Biochemistry · 2014Article
- Activation of IP3 receptors requires an endogenous 1-8-14 calmodulin-binding motif.The Biochemical journal · 2013Article
- Enhanced binding of calmodulin to the ryanodine receptor corrects contractile dysfunction in failing hearts.Cardiovascular research · 2012Article
- Aberrant interaction of calmodulin with the ryanodine receptor develops hypertrophy in the neonatal cardiomyocyte.The Biochemical journal · 2011Article
- The IQ motif is crucial for Cav1.1 function.Journal of biomedicine & biotechnology · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
A fragment of RyR1 (amino acids 4064-4210) is predicted to fold to at least one lobe of calmodulin and to bind Ca(2+). This fragment of RyR1 (R4064-4210) was subcloned, expressed, refolded, and purified. Consistent with the predicted folding pattern, R4064-4210 was found to bind two molecules of Ca(2+) and undergo a structural change upon binding Ca(2+) that exposes hydrophobic amino acids. R4064-4210 also binds to RyR1, the L-type Ca(2+) channel (Cav(1.1)), and several synthetic calmodulin binding peptides. Both R4064-4210 and a peptide representing the calmodulin-binding region of RyR1 (R3614-3643) alter the Ca(2+) dependence of ((3)H)ryanodine binding to RyR1, suggesting that they may both be interfering with an intramolecular interaction between amino acids 4064-4210 and amino acids 3614-3643 in the native RyR1 to alter or regulate the response of the channel to changes in Ca(2+) concentration. The finding that a domain within RyR1 binds Ca(2+) and interacts with calmodulin-binding motifs may provide insights into the mechanism for calcium- and calmodulin-dependent regulation of this channel and perhaps for its regulation by the L-type Ca(2+) channel.
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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.