ArticleThe Journal of cell biology1999
Type 3 and type 1 ryanodine receptors are localized in triads of the same mammalian skeletal muscle fibers.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 72 citations in OpenAlex.
- Sequential Gating of Ryanodine Receptors Underlies the Development of Calcium Sparks in Frog Skeletal Muscle.Biomolecules · 2026Article
- Reactive oxygen species in the pathogenesis of sarcopenia.Free radical biology & medicine · 2025Review
- Detection of Ca2+ transients near ryanodine receptors by targeting fluorescent Ca2+ sensors to the triad.The Journal of general physiology · 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
- The structural basis of ryanodine receptor ion channel function.The Journal of general physiology · 2017Review
- In vivo CaPhysiological reports · 2017Article
- Observation of Network Dynamics of Ryanodine Receptors on Skeletal Muscle Sarcoplasmic Reticulum Membranes.European journal of translational myology · 2016Article
- Observation of the molecular organization of calcium release sites in fast- and slow-twitch skeletal muscle with nanoscale imaging.Journal of the Royal Society, Interface · 2014Article
- Stable incorporation versus dynamic exchange of β subunits in a native Ca2+ channel complex.Journal of cell science · 2013Article
- Visualization of Ca²+ signaling during embryonic skeletal muscle formation in vertebrates.Cold Spring Harbor perspectives in biology · 2011Review
- Selenoprotein N is dynamically expressed during mouse development and detected early in muscle precursors.BMC developmental biology · 2009Article
- Obscurin interacts with a novel isoform of MyBP-C slow at the periphery of the sarcomeric M-band and regulates thick filament assembly.Molecular biology of the cell · 2009Article
- Spontaneous and voltage-activated Ca2+ release in adult mouse skeletal muscle fibres expressing the type 3 ryanodine receptor.The Journal of physiology · 2008Article
- Article
- Simulation of Ca2+ movements within the sarcomere of fast-twitch mouse fibers stimulated by action potentials.The Journal of general physiology · 2007Article
- RyR isoforms and fibre type-specific expression of proteins controlling intracellular calcium concentration in skeletal muscles.Journal of muscle research and cell motility · 2006Review
- External Ca(2+)-dependent excitation--contraction coupling in a population of ageing mouse skeletal muscle fibres.The Journal of physiology · 2004Article
- The elementary events of Ca2+ release elicited by membrane depolarization in mammalian muscle.The Journal of physiology · 2004Article
- Ca2+-dependent excitation-contraction coupling triggered by the heterologous cardiac/brain DHPR beta2a-subunit in skeletal myotubes.Biophysical journal · 2003Article
- Ca2+ sparks and embers of mammalian muscle. Properties of the sources.The Journal of general physiology · 2003Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The type 3 ryanodine receptor (RyR3) is a ubiquitous calcium release channel that has recently been found in mammalian skeletal muscles. However, in contrast to the skeletal muscle isoform (RyR1), neither the subcellular distribution nor the physiological role of RyR3 are known. Here, we used isoform-specific antibodies to localize RyR3 in muscles of normal and RyR knockout mice. In normal hind limb and diaphragm muscles of young mice, RyR3 was expressed in all fibers where it was codistributed with RyR1 and with the skeletal muscle dihydropyridine receptor. This distribution pattern indicates that RyR3 is localized in the triadic junctions between the transverse tubules and the sarcoplasmic reticulum. During development, RyR3 expression declined rapidly in some fibers whereas other fibers maintained expression of RyR3 into adulthood. Comparing the distribution of RyR3-containing fibers with that of known fiber types did not show a direct correlation. Targeted deletion of the RyR1 or RyR3 gene resulted in the expected loss of the targeted isoform, but had no adverse effects on the expression and localization of the respective other RyR isoform. The localization of RyR3 in skeletal muscle triads, together with RyR1, is consistent with an accessory function of RyR3 in skeletal muscle excitation-contraction coupling.
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