ArticleThe Journal of cell biology1998
Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 143 citations in OpenAlex.
- Review
- An aged-related structural study of DHPR tetrads in peripheral couplings of human skeletal muscle.European journal of translational myology · 2024Article
- Synthesis and Insecticidal Activity of Novel Anthranilic Diamide Insecticides Containing Indane and Its Analogs.International journal of molecular sciences · 2024Article
- Ablation of Calsequestrin-1, CaFrontiers in physiology · 2022Review
- Multi-Scale Computational Modeling of Spatial Calcium Handling From Nanodomain to Whole-Heart: Overview and Perspectives.Frontiers in physiology · 2022Review
- Pannexin-1 and CaV1.1 show reciprocal interaction during excitation-contraction and excitation-transcription coupling in skeletal muscle.The Journal of general physiology · 2021Article
- Improper Remodeling of Organelles Deputed to CaInternational journal of molecular sciences · 2021Review
- Calcium entry units (CEUs): perspectives in skeletal muscle function and disease.Journal of muscle research and cell motility · 2021Article
- 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
- Junctional trafficking and restoration of retrograde signaling by the cytoplasmic RyR1 domain.The Journal of general physiology · 2018Article
- De novo reconstitution reveals the proteins required for skeletal muscle voltage-induced CaProceedings of the National Academy of Sciences of the United States of America · 2017Article
- The structural basis of ryanodine receptor ion channel function.The Journal of general physiology · 2017Review
- The Central domain of RyR1 is the transducer for long-range allosteric gating of channel opening.Cell research · 2016Article
- Comparative Transcriptomic Study of Muscle Provides New Insights into the Growth Superiority of a Novel Grouper Hybrid.PloS one · 2016Article
- Structural and functional properties of ryanodine receptor type 3 in zebrafish tail muscle.The Journal of general physiology · 2015Article
- Stac adaptor proteins regulate trafficking and function of muscle and neuronal L-type Ca2+ channels.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- 3D Structure of the Dihydropyridine Receptor of Skeletal Muscle.European journal of translational myology · 2015Review
- Amino acid residues 489-503 of dihydropyridine receptor (DHPR) β1a subunit are critical for structural communication between the skeletal muscle DHPR complex and type 1 ryanodine receptor.The Journal of biological chemistry · 2014Article
- Friends of Physiology: an interview with Clara Franzini-Armstrong and Clay Armstrong.The Journal of general physiology · 2013Article
- Ca(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channel.Biochimica et biophysica acta · 2013Review
4 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
In muscle cells, excitation-contraction (e-c) coupling is mediated by "calcium release units," junctions between the sarcoplasmic reticulum (SR) and exterior membranes. Two proteins, which face each other, are known to functionally interact in those structures: the ryanodine receptors (RyRs), or SR calcium release channels, and the dihydropyridine receptors (DHPRs), or L-type calcium channels of exterior membranes. In skeletal muscle, DHPRs form tetrads, groups of four receptors, and tetrads are organized in arrays that face arrays of feet (or RyRs). Triadin is a protein of the SR located at the SR-exterior membrane junctions, whose role is not known. We have structurally characterized calcium release units in a skeletal muscle cell line (1B5) lacking Ry1R. Using immunohistochemistry and freeze-fracture electron microscopy, we find that DHPR and triadin are clustered in foci in differentiating 1B5 cells. Thin section electron microscopy reveals numerous SR-exterior membrane junctions lacking foot structures (dyspedic). These results suggest that components other than Ry1Rs are responsible for targeting DHPRs and triadin to junctional regions. However, DHPRs in 1B5 cells are not grouped into tetrads as in normal skeletal muscle cells suggesting that anchoring to Ry1Rs is necessary for positioning DHPRs into ordered arrays of tetrads. This hypothesis is confirmed by finding a "restoration of tetrads" in junctional domains of surface membranes after transfection of 1B5 cells with cDNA encoding for Ry1R.
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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.