Physiological role for S-nitrosylation of RyR1 in skeletal muscle function and development.

ABSTRACT: Excitation-contraction coupling in skeletal muscle myofibers depends upon Ca²⁺ release from the sarcoplasmic reticulum through the ryanodine receptor/Ca²⁺-release channel RyR1. The RyR1 contains ∼100 Cys thiols of which ∼30 comprise an allosteric network subject to posttranslational modification by S-nitrosylation, S-palmitoylation and S-oxidation. However, the role and function of these modifications is not understood. Although aberrant S-nitrosylation of multiple unidentified sites has been associated with dystrophic diseases, malignant hyperthermia and other myopathic syndromes, S-nitrosylation in physiological situations is reportedly specific to a single (1 of ∼100) Cys in RyR1, Cys³⁶³⁶ in a manner gated by pO₂. Using mice expressing a form

SUBMITTER: Sun QA 

PROVIDER: S-EPMC12651786 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature