Abstract
The ryanodine receptor (RyR) is a Ca2+ release channel in the sarcoplasmic reticulum of skeletal and cardiac muscles and plays a key role in excitation–contraction coupling. The activity of the RyR is regulated by the changes in the level of many intracellular factors, such as divalent cations (Ca2+ and Mg2+), nucleotides, associated proteins, and reactive oxygen species. Since these intracellular factors change depending on the condition of the muscle, e.g., exercise, fatigue, or disease states, the RyR channel activity will be altered accordingly. In this review, we describe how the RyR channel is regulated under various conditions and discuss the possibility that the RyR acts as a sensor for changes in the intracellular environments in muscles.
Highlights
Skeletal and cardiac muscles are essential organs for the maintenance of life, which embody most of the daily activities, such as walking, eating, and creating
RyR2 oxidation and S-nitrosylation and FKBP12.6 dissociation, muscle is subjected to high-load exercise, the channel activity becomes reduced by alteration of nucleotide composition
Since ryanodine receptor (RyR) are submaximally active under normal muscle conditions, they can sense changes in the intracelluturn may lead to increased Ca2+ spark frequency and development of tachycardia [148]
Summary
Skeletal and cardiac muscles are essential organs for the maintenance of life, which embody most of the daily activities, such as walking, eating, and creating. The RyR1 channel opening is triggered by a conformational change in the DHPR after depolarization of the T-tubule (referred to as depolarization-induced Ca2+ release, DICR) [1,2,3]. The S2–S3 domain, which is the region between S2 and S3 helices on the cytosolic side, is thought to be involved in regulation of channel opening. 2021, 22, x FOR PEER REVIEW disease-linked point mutations have been identified in RyR cytoplasmic domains, this region is thought to be involved in the regulation of channel activity [13].
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