ArticleBiophysical journal2003
RyR1/RyR3 chimeras reveal that multiple domains of RyR1 are involved in skeletal-type E-C coupling.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 40 citations in OpenAlex.
- Cryo-EM investigation of ryanodine receptor type 3.Nature communications · 2024Article
- Excitation-contraction coupling in skeletal muscle: recent progress and unanswered questions.Biophysical reviews · 2020Review
- High Time Resolution Analysis of Voltage-Dependent and Voltage-Independent Calcium Sparks in Frog Skeletal Muscle Fibers.Frontiers in physiology · 2020Article
- Distinct Components of Retrograde Ca(V)1.1-RyR1 Coupling Revealed by a Lethal Mutation in RyR1.Biophysical journal · 2016Article
- Ryanodine receptor 2 contributes to hemorrhagic shock-induced bi-phasic vascular reactivity in rats.Acta pharmacologica Sinica · 2014Article
- Myoplasmic resting Ca2+ regulation by ryanodine receptors is under the control of a novel Ca2+-binding region of the receptor.The Biochemical journal · 2014Article
- Alteration of Ryanodine-receptors in Cultured Rat Aortic Smooth Muscle Cells.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2011Article
- Ubiquitous SPRY domains and their role in the skeletal type ryanodine receptor.European biophysics journal : EBJ · 2009Review
- Role of ryanodine receptor subtypes in initiation and formation of calcium sparks in arterial smooth muscle: comparison with striated muscle.Journal of biomedicine & biotechnology · 2009Review
- Allosterically coupled calcium and magnesium binding sites are unmasked by ryanodine receptor chimeras.Biochemical and biophysical research communications · 2008Article
- Maurocalcine interacts with the cardiac ryanodine receptor without inducing channel modification.The Biochemical journal · 2007Article
- Bridging the myoplasmic gap: recent developments in skeletal muscle excitation-contraction coupling.Journal of muscle research and cell motility · 2007Review
- Bidirectional signaling between calcium channels of skeletal muscle requires multiple direct and indirect interactions.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Effects of peptide C corresponding to the Glu724-Pro760 region of the II-III loop of the DHP (dihydropyridine) receptor alpha1 subunit on the domain- switch-mediated activation of RyR1 (ryanodine receptor 1) Ca2+ channels.The Biochemical journal · 2006Article
- Localization of a disease-associated mutation site in the three-dimensional structure of the cardiac muscle ryanodine receptor.The Journal of biological chemistry · 2005Article
- Evidence for conformational coupling between two calcium channels.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Ca2+-dependent excitation-contraction coupling triggered by the heterologous cardiac/brain DHPR beta2a-subunit in skeletal myotubes.Biophysical journal · 2003Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Skeletal-type E-C coupling is thought to require a direct interaction between RyR1 and the alpha(1S)-DHPR. Most available evidence suggests that the cytoplasmic II-III loop of the dihydropyridine receptor (DHPR) is the primary source of the orthograde signal. However, identification of the region(s) of RyR1 involved in bidirectional signaling with the alpha(1S)-DHPR remains elusive. To identify these regions we have designed a series of chimeric RyR cDNAs in which different segments of RyR1 were inserted into the corresponding region of RyR3 and expressed in dyspedic 1B5 myotubes. RyR3 provides a preferable background than RyR2 for defining domains essential for E-C coupling because it possesses less sequence homology to RyR1 than the RyR2 backbone used in previous studies. Our data show that two regions of RyR1 (chimera Ch-10 aa 1681-2641 and Ch-9 aa 2642-3770), were independently able to restore skeletal-type E-C coupling to RyR3. These two regions were further mapped and the critical RyR1 residues were 1924-2446 (Ch-21) and 2644-3223 (Ch-19). These results both support and refine the previous hypothesis that multiple domains of RyR1 combine to functionally interact with the DHPR during E-C coupling.
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