ArticleThe Journal of biological chemistry2008
Single channel properties of heterotetrameric mutant RyR1 ion channels linked to core myopathies.
Article in The Journal of biological chemistry, 2008. 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, 39 citations in OpenAlex.
- Article
- Ex Vivo Single-molecule Analysis of Ryanodine Receptor 2 Assembly in Cardiac and Neuronal Tissue.Journal of visualized experiments : JoVE · 2025Article
- Quantitative Single-Molecule Analysis of Ryanodine Receptor 2 Subunit Assembly in Cardiac and Neuronal Tissues.Analytical chemistry · 2024Article
- Mutations in proteins involved in E-C coupling and SOCE and congenital myopathies.The Journal of general physiology · 2022Review
- Core myopathies - a short review.Acta myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology · 2020Review
- Preclinical model systems of ryanodine receptor 1-related myopathies and malignant hyperthermia: a comprehensive scoping review of works published 1990-2019.Orphanet journal of rare diseases · 2020Article
- Single-channel properties of skeletal muscle ryanodine receptor pore ΔCell calcium · 2020Article
- A central core disease mutation in the CaAmerican journal of physiology. Cell physiology · 2019Article
- 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
- The structural basis of ryanodine receptor ion channel function.The Journal of general physiology · 2017Review
- Unexpected dependence of RyR1 splice variant expression in human lower limb muscles on fiber-type composition.Pflugers Archiv : European journal of physiology · 2016Article
- Interaction of ions with the luminal sides of wild-type and mutated skeletal muscle ryanodine receptors.Journal of molecular modeling · 2016Article
- Channel Gating Dependence on Pore Lining Helix Glycine Residues in Skeletal Muscle Ryanodine Receptor.The Journal of biological chemistry · 2015Article
- Pore dynamics and conductance of RyR1 transmembrane domain.Biophysical journal · 2014Article
- Genetic ablation of ryanodine receptor 2 phosphorylation at Ser-2808 aggravates Ca(2+)-dependent cardiomyopathy by exacerbating diastolic Ca2+ release.The Journal of physiology · 2014Article
- Ca2+ release in muscle fibers expressing R4892W and G4896V type 1 ryanodine receptor disease mutants.PloS one · 2013Article
- Two-pore channels form homo- and heterodimers.The Journal of biological chemistry · 2011Article
- Calcitonin gene-related peptide restores disrupted excitation-contraction coupling in myotubes expressing central core disease mutations in RyR1.The Journal of physiology · 2011Article
- Muscle weakness in Ryr1I4895T/WT knock-in mice as a result of reduced ryanodine receptor Ca2+ ion permeation and release from the sarcoplasmic reticulum.The Journal of general physiology · 2011Article
- The I4895T mutation in the type 1 ryanodine receptor induces fiber-type specific alterations in skeletal muscle that mimic premature aging.Aging cell · 2010Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Skeletal muscle excitation-contraction coupling involves activation of homotetrameric ryanodine receptor ion channels (RyR1s), resulting in the rapid release of Ca(2+) from the sarcoplasmic reticulum. Previous work has shown that Ca(2+) release is impaired by mutations in RyR1 linked to Central Core Disease and Multiple Minicore Disease. We studied the consequences of these mutations on RyR1 function, following their expression in human embryonic kidney 293 cells and incorporation in lipid bilayers. RyR1-G4898E, -G4898R, and -DeltaV4926/I4927 mutants in the C-terminal pore region of RyR1 and N-terminal RyR1-R110W/L486V mutant all showed negligible Ca(2+) permeation and loss of Ca(2+)-dependent channel activity but maintained reduced K(+) conductances. Co-expression of wild type and mutant RyR1s resulted in Ca(2+)-dependent channel activities that exhibited intermediate Ca(2+) selectivities compared with K(+), which suggested the presence of tetrameric RyR1 complexes composed of wild type and mutant subunits. The number of wild-type subunits to maintain a functional heterotetrameric channel differed among the four RyR1 mutants. The results indicate that homozygous RyR1 mutations associated with core myopathies abolish or greatly reduce sarcoplasmic reticulum Ca(2+) release during excitation-contraction coupling. They further suggest that in individuals, expressing wild type and mutant alleles, a substantial portion of RyR1 channels is able to release Ca(2+) from sarcoplasmic reticulum.
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