ArticleThe Journal of biological chemistry2015
Characterization of Two Human Skeletal Calsequestrin Mutants Implicated in Malignant Hyperthermia and Vacuolar Aggregate Myopathy.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
- Vacuolar myopathy caused by CASQ1 p.Asp244His: pathogenic evidence from two unrelated Chinese families.Journal of human genetics · 2026Article
- STIM1 GoF Mutants: Genotype-Phenotype Relationships Across the Stormorken/TAM/YPS Spectrum.Cells · 2026Review
- Characterization of novel CASQ1 variants in two families with unusual phenotypic features.Journal of neurology · 2025Article
- TAM-associated CASQ1 mutants diminish intracellular CaJournal of muscle research and cell motility · 2024Article
- The Structural-Functional Crosstalk of the Calsequestrin System: Insights and Pathological Implications.Biomolecules · 2023Review
- Physiology of intracellular calcium buffering.Physiological reviews · 2023Review
- Sarcoplasmic Reticulum CaCells · 2023Review
- CASQ1-related myopathy: The first report from China and the literature review.Clinical case reports · 2022Article
- Calsequestrin 1 Is an Active Partner of Stromal Interaction Molecule 2 in Skeletal Muscle.Cells · 2021Article
- Calsequestrin, a key protein in striated muscle health and disease.Journal of muscle research and cell motility · 2021Review
- Pathological mechanisms of vacuolar aggregate myopathy arising from a Casq1 mutation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- Calsequestrin: a well-known but curious protein in skeletal muscle.Experimental & molecular medicine · 2020Review
- The structure of a calsequestrin filament reveals mechanisms of familial arrhythmia.Nature structural & molecular biology · 2020Article
- The clinical spectrum ofNeurology · 2018Article
- Sarcoplasmic reticulum CaJournal of molecular and cellular cardiology · 2017Article
- 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
- Excitation-Contraction Coupling Alterations in Myopathies.Journal of neuromuscular diseases · 2016Review
- Characterization of Post-Translational Modifications to Calsequestrins of Cardiac and Skeletal Muscle.International journal of molecular sciences · 2016Article
- Single-molecule Force Spectroscopy Reveals the Calcium Dependence of the Alternative Conformations in the Native State of a βγ-Crystallin Protein.The Journal of biological chemistry · 2016Article
- Muscle Decline in Aging and Neuromuscular Disorders - Mechanisms and Countermeasures: Terme Euganee, Padova (Italy), April 13-16, 2016.European journal of translational myology · 2016Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Calsequestrin 1 is the principal Ca(2+) storage protein of the sarcoplasmic reticulum of skeletal muscle. Its inheritable D244G mutation causes a myopathy with vacuolar aggregates, whereas its M87T "variant" is weakly associated with malignant hyperthermia. We characterized the consequences of these mutations with studies of the human proteins in vitro. Equilibrium dialysis and turbidity measurements showed that D244G and, to a lesser extent, M87T partially lose Ca(2+) binding exhibited by wild type calsequestrin 1 at high Ca(2+) concentrations. D244G aggregates abruptly and abnormally, a property that fully explains the protein inclusions that characterize its phenotype. D244G crystallized in low Ca(2+) concentrations lacks two Ca(2+) ions normally present in wild type that weakens the hydrophobic core of Domain II. D244G crystallized in high Ca(2+) concentrations regains its missing ions and Domain II order but shows a novel dimeric interaction. The M87T mutation causes a major shift of the α-helix bearing the mutated residue, significantly weakening the back-to-back interface essential for tetramerization. D244G exhibited the more severe structural and biophysical property changes, which matches the different pathophysiological impacts of these mutations.
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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.