ArticleCell calcium2011
Reduced gain of excitation-contraction coupling in triadin-null myotubes is mediated by the disruption of FKBP12/RyR1 interaction.
Article in Cell calcium, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Interactive Role of the DHPR βBiomolecules · 2025Article
- Article
- Using CaPsychopharmacology · 2019Review
- Functional and structural characterization of a novel malignant hyperthermia-susceptible variant of DHPR-βAmerican journal of physiology. Cell physiology · 2018Article
- Three residues in the luminal domain of triadin impact on Trisk 95 activation of skeletal muscle ryanodine receptors.Pflugers Archiv : European journal of physiology · 2016Article
- Electrical coupling between the human serotonin transporter and voltage-gated Ca(2+) channels.Cell calcium · 2014Article
- FKBP12.6 activates RyR1: investigating the amino acid residues critical for channel modulation.Biophysical journal · 2014Article
- Article
- Reciprocal dihydropyridine and ryanodine receptor interactions in skeletal muscle activation.Journal of muscle research and cell motility · 2011Review
- On the footsteps of Triadin and its role in skeletal muscle.World journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Several studies have suggested that triadin (Tdn) may be a critical component of skeletal EC-coupling. However, using Tdn-null mice we have shown that triadin ablation results in no significant disruption of skeletal EC-coupling. To analyze the role of triadin in EC-coupling signaling here we used whole-cell voltage clamp and simultaneous recording of intracellular Ca²+ release to characterize the retrograde and orthograde signaling between RyR1 and DHPR in cultured myotubes. DHPR Ca²+ currents elicited by depolarization of Wt and Tdn-null myotubes displayed similar current densities and voltage dependence. However, kinetic analysis of the Ca²+ current shows that activation time constant of the slow component was slightly decreased in Tdn-null cells. Voltage-evoked Ca²+ transient of Tdn-null myotubes showed small but significant reduction in peak fluorescence amplitude but no differences in voltage dependence. This difference in Ca²+ amplitude was averted by over-expression of FKBP12.6. Our results show that bi-directional signaling between DHPR and RyR1 is preserved nearly intact in Tdn-null myotubes and that the effect of triadin ablation on Ca²+ transients appears to be secondary to the reduced FKBP12 binding capacity of RyR1 in Tdn-null myotubes. These data suggest that skeletal triadins do not play a direct role in skeletal EC-coupling.
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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.