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Cover Image
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ON THE COVER
Electron microscopy of EDL and soleus muscles from WT and transgenic mice carrying the homozygous RyR1 p.F4976L mutation. Dark arrows point to calcium release units, and empty arrow points to focal areas of myofibrillar degeneration present in muscles from homozygous mice. Image © Benucci et al., 2024. See https://doi.org/10.1085/jgp.202313486. - PDF Icon PDF LinkTable of Contents
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Research News
RyR2 phosphorylation alters dyad architecture
JGP study indicates that β-adrenergic signaling enlarges dyads and reorganizes RyR2 tetramers in cardiomyocytes.
Articles
Phosphorylation of RyR2 simultaneously expands the dyad and rearranges the tetramers
Asghari et al. analyzed a series of RyR2 phosphorylation mutants, all of which altered the structure of the dyad and its response to the β-agonist isoproterenol. Their results suggest a direct link between the phosphorylation state of the channel tetramer and the microarchitecture of the dyad.
Tirasemtiv enhances submaximal muscle tension in an Acta1:p.Asp286Gly mouse model of nemaline myopathy
Acute and long-term treatment with tirasemtiv, a fast troponin skeletal muscle activator, improves skeletal and respiratory muscle function in a mouse model for nemaline myopathy type 3, caused by a p.Asp286Cys variant in ACTA1.
A novel, patient-derived RyR1 mutation impairs muscle function and calcium homeostasis in mice
Benucci et al. characterize a new mouse model carrying a mutation in RyR1 identified in a severely affected child. Their model reveals that homozygosity for this pathophysiologically relevant mutation functionally impacts muscle function and alters calcium homeostasis.
