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Orai1 inhibitor STIM2β regulates myogenesis by controlling SOCE dependent transcriptional factors.

Sci Rep. 2019 Jul 25;9(1):10794
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摘要


Store-operated Ca2+ entry (SOCE), the fundamental Ca2+ signaling mechanism in myogenesis, is mediated by stromal interaction molecule (STIM), which senses the depletion of endoplasmic reticulum Ca2+ stores and induces Ca2+ influx by activating Orai channels in the plasma membrane. Recently, STIM2β, an eight-residue-inserted splice variant of STIM2, was found to act as an inhibitor of SOCE. Although a previous study demonstrated an increase in STIM2β splicing during in vitro differentiation of skeletal muscle, the underlying mechanism and detailed function of STIM2β in myogenesis remain unclear. In this study, we investigated the function of STIM2β in myogenesis using the C2C12 cell line with RNA interference-mediated knockdown and CRISPR-Cas-mediated knockout approaches. Deletion of STIM2β delayed myogenic differentiation through the MEF2C and NFAT4 pathway in C2C12 cells. Further, loss of STIM2β increased cell proliferation by altering Ca2+ homeostasis and inhibited cell cycle arrest mediated by the cyclin D1-CDK4 degradation pathway. Thus, this study identified a previously unknown function of STIM2β in myogenesis and improves the understanding of how cells effectively regulate the development process via alternative splicing.

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