What is it about?
Ionized calcium serves as an essential intracellular messenger in multiple cell signaling pathways mediating various biological functions. In heart and skeletal muscle, the small calcium binding protein S100A1 modulates intracellular calcium transients determining muscle contractile performance. One key regulatory interaction target of S100A1 is the ryanodine receptor (RyR) that forms intracellular calcium release channels crucial for calcium signaling. Our work provides a structural and functional characterization of the interaction between S100A1 and skeletal muscle type-1 RyR. Importantly, calcium-dependent differences are revealed in S100A1 binding poses on RyR1 channels, which are involved in calcium signal transductions.
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Why is it important?
Dysregulated RyR channels are associated with disturbed calcium signaling and abnormal muscle function, which can lead to myopathies or heart failure. The regulation of RyR channels by S100A1 may serve as a promising target for therapeutic strategies regarding treatments of RyR-related disorders.
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This page is a summary of: Structural insights into the regulation of RyR1 by S100A1, Proceedings of the National Academy of Sciences, June 2024, Proceedings of the National Academy of Sciences,
DOI: 10.1073/pnas.2400497121.
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