ArticleThe Journal of general physiology2011
Measurement of RyR permeability reveals a role of calsequestrin in termination of SR Ca(2+) release in skeletal muscle.
Article in The Journal of general physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 49 citations in OpenAlex.
- Modeling the mechanism of Ca2+ release in skeletal muscle by DHPRs easing inhibition at RyR I1-sites.The Journal of general physiology · 2024Article
- Quantal Properties of Voltage-Dependent CaThe Journal of membrane biology · 2024Article
- Physiology of intracellular calcium buffering.Physiological reviews · 2023Review
- A mathematical model to quantify RYR Ca2+ leak and associated heat production in resting human skeletal muscle fibers.The Journal of general physiology · 2022Article
- Article
- Altered CaMetabolites · 2021Review
- Calsequestrin, a key protein in striated muscle health and disease.Journal of muscle research and cell motility · 2021Review
- Detection of Ca2+ transients near ryanodine receptors by targeting fluorescent Ca2+ sensors to the triad.The Journal of general physiology · 2021Article
- Article
- Calsequestrin: a well-known but curious protein in skeletal muscle.Experimental & molecular medicine · 2020Review
- Pre-assembled Ca2+ entry units and constitutively active Ca2+ entry in skeletal muscle of calsequestrin-1 knockout mice.The Journal of general physiology · 2020Article
- ECC meets CEU-New focus on the backdoor for calcium ions in skeletal muscle cells.The Journal of general physiology · 2020Article
- Tracking the sarcoplasmic reticulum membrane voltage in muscle with a FRET biosensor.The Journal of general physiology · 2018Article
- A study of the mechanisms of excitation-contraction coupling in frog skeletal muscle based on measurements of [CaJournal of muscle research and cell motility · 2018Review
- The relationship between form and function throughout the history of excitation-contraction coupling.The Journal of general physiology · 2018Review
- Article
- The structural basis of ryanodine receptor ion channel function.The Journal of general physiology · 2017Review
- Calsequestrin depolymerizes when calcium is depleted in the sarcoplasmic reticulum of working muscle.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Role of the JP45-Calsequestrin Complex on Calcium Entry in Slow Twitch Skeletal Muscles.The Journal of biological chemistry · 2016Article
- Characterization of Two Human Skeletal Calsequestrin Mutants Implicated in Malignant Hyperthermia and Vacuolar Aggregate Myopathy.The Journal of biological chemistry · 2015Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The mechanisms that terminate Ca(2+) release from the sarcoplasmic reticulum are not fully understood. D4cpv-Casq1 (Sztretye et al. 2011. J. Gen. Physiol. doi:10.1085/jgp.201010591) was used in mouse skeletal muscle cells under voltage clamp to measure free Ca(2+) concentration inside the sarcoplasmic reticulum (SR), [Ca(2+)](SR), simultaneously with that in the cytosol, [Ca(2+)](c), during the response to long-lasting depolarization of the plasma membrane. The ratio of Ca(2+) release flux (derived from [Ca(2+)](c)(t)) over the gradient that drives it (essentially equal to [Ca(2+)](SR)) provided directly, for the first time, a dynamic measure of the permeability to Ca(2+) of the releasing SR membrane. During maximal depolarization, flux rapidly rises to a peak and then decays. Before 0.5 s, [Ca(2+)](SR) stabilized at ∼35% of its resting level; depletion was therefore incomplete. By 0.4 s of depolarization, the measured permeability decayed to ∼10% of maximum, indicating ryanodine receptor channel closure. Inactivation of the t tubule voltage sensor was immeasurably small by this time and thus not a significant factor in channel closure. In cells of mice null for Casq1, permeability did not decrease in the same way, indicating that calsequestrin (Casq) is essential in the mechanism of channel closure and termination of Ca(2+) release. The absence of this mechanism explains why the total amount of calcium releasable by depolarization is not greatly reduced in Casq-null muscle (Royer et al. 2010. J. Gen. Physiol. doi:10.1085/jgp.201010454). When the fast buffer BAPTA was introduced in the cytosol, release flux became more intense, and the SR emptied earlier. The consequent reduction in permeability accelerated as well, reaching comparable decay at earlier times but comparable levels of depletion. This observation indicates that [Ca(2+)](SR), sensed by Casq and transmitted to the channels presumably via connecting proteins, is determinant to cause the closure that terminates Ca(2+) release.
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