Alexander Sonne, Anna Katarina Antonovic, Elise Melhedegaard, Fariha Akter, Jesper L. Andersen, Heinz Jungbluth, Nanna Witting, John Vissing, Edmar Zanoteli, Arianna Fornili, Julien Ochala
Conditions related to mutations in the gene encoding the skeletal muscle
ryanodine receptor 1 (RYR1) are genetic muscle disorders and include congenital myopathies with permanent weakness, as well as episodic phenotypes such
as rhabdomyolysis/myalgia. Although RYR1 dysfunction is the primary mechanism in RYR1-related disorders, other downstream pathogenic events are less
well understood and may include a secondary remodeling of major contractile
proteins. Hence, in the present study, we aimed to investigate whether congenital myopathy-related RYR1 mutations alter the regulation of the most abundant
contractile protein, myosin.