ArticleJournal of cell science2015
A new cytoplasmic interaction between junctin and ryanodine receptor Ca2+ release channels.
Article in Journal of cell science, 2015. 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, 24 citations in OpenAlex.
- Molecular genetics of skeletal muscle diseases associated with abnormal excitation-contraction coupling.Journal of human genetics · 2026Review
- JP2 and JCN Crosstalk Abrogate MURF1-Mediated JCN Ubiquitination and Degradation in Cardiomyocytes.JACC. Basic to translational science · 2026Article
- Structural and Functional Regulation of RyR2 in Cardiac Calcium Handling and Arrhythmogenesis.Biomedicines · 2026Review
- Nonstructural Roles of Junctophilin-2 in the Heart.JACC. Basic to translational science · 2025Review
- Structural insights into transmembrane helix S0 facilitated RyR1 channel gating by CaNature communications · 2025Article
- Identification and Characterization of Extrachromosomal Circular DNA in Slimming Grass Carp.Biomolecules · 2024Article
- Detoxification and benefits on acute heart failure in mice- of fuziline using glycyrrhetinic acid: an integrated biochemical analysis.Frontiers in pharmacology · 2024Article
- The Dysfunction of CaInternational journal of molecular sciences · 2023Review
- FKBP12 binds to the cardiac ryanodine receptor with negative cooperativity: implications for heart muscle physiology in health and disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Article
- Three-dimensional perspective on ryanodine receptor mutations causing skeletal and cardiac muscle-related diseases.Current opinion in pharmacology · 2023Review
- Shank3 related muscular hypotonia is accompanied by increased intracellular calcium concentrations and ion channel dysregulation in striated muscle tissue.Frontiers in cell and developmental biology · 2023Article
- How does flecainide impact RyR2 channel function?The Journal of general physiology · 2022Article
- Mutations in proteins involved in E-C coupling and SOCE and congenital myopathies.The Journal of general physiology · 2022Review
- Variants in ASPH cause exertional heat illness and are associated with malignant hyperthermia susceptibility.Nature communications · 2022Article
- The Sarcoplasmic Reticulum of Skeletal Muscle Cells: A Labyrinth of Membrane Contact Sites.Biomolecules · 2022Review
- Ablation of Calsequestrin-1, CaFrontiers in physiology · 2022Review
- Structural Insight Into Ryanodine Receptor Channelopathies.Frontiers in pharmacology · 2022Review
- RyR1-related myopathy mutations in ATP and calcium binding sites impair channel regulation.Acta neuropathologica communications · 2021Article
- The structural basis of ryanodine receptor ion channel function.The Journal of general physiology · 2017Review
- Synthesis of the CaThe Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Junctin, a non-catalytic splice variant encoded by the aspartate-β-hydroxylase (Asph) gene, is inserted into the membrane of the sarcoplasmic reticulum (SR) Ca(2+) store where it modifies Ca(2+) signalling in the heart and skeletal muscle through its regulation of ryanodine receptor (RyR) Ca(2+) release channels. Junctin is required for normal muscle function as its knockout leads to abnormal Ca(2+) signalling, muscle dysfunction and cardiac arrhythmia. However, the nature of the molecular interaction between junctin and RyRs is largely unknown and was assumed to occur only in the SR lumen. We find that there is substantial binding of RyRs to full junctin, and the junctin luminal and, unexpectedly, cytoplasmic domains. Binding of these different junctin domains had distinct effects on RyR1 and RyR2 activity: full junctin in the luminal solution increased RyR channel activity by ∼threefold, the C-terminal luminal interaction inhibited RyR channel activity by ∼50%, and the N-terminal cytoplasmic binding produced an ∼fivefold increase in RyR activity. The cytoplasmic interaction between junctin and RyR is required for luminal binding to replicate the influence of full junctin on RyR1 and RyR2 activity. The C-terminal domain of junctin binds to residues including the S1-S2 linker of RyR1 and N-terminal domain of junctin binds between RyR1 residues 1078 and 2156.
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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.