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Review
. 2020 Nov 6:11:583393.
doi: 10.3389/fphys.2020.583393. eCollection 2020.

Multi-Cellular Functions of MG53 in Muscle Calcium Signaling and Regeneration

Dathe Z Benissan-Messan  1 , Hua Zhu  1 , Weina Zhong  1 , Tao Tan  1 , Jianjie Ma  1 , Peter H U Lee  1   2   3
Affiliations
Review

Multi-Cellular Functions of MG53 in Muscle Calcium Signaling and Regeneration

Dathe Z Benissan-Messan et al. Front Physiol. .

Abstract

Since its identification in 2009, multiple studies have indicated the importance of MG53 in muscle physiology. The protein is produced in striated muscles but has physiologic implications reaching beyond the confines of striated muscles. Roles in muscle regeneration, calcium homeostasis, excitation-contraction coupling, myogenesis, and the mitochondria highlight the protein's wide-reaching impact. Numerous therapeutic applications could potentially emerge from these physiologic roles. This review summarizes the current literature regarding the role of MG53 in the skeletal muscle. Therapeutic applications are discussed.

Keywords: TRIM72; calcium homeostasis; insulin resistance; metabolic syndrome; mitochondria; myogenesis; plasma membrane repair; skeletal muscle regeneration.

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Figures

FIGURE 1
FIGURE 1
(A) MG53 controls cytosolic calcium through interactions with Orai1, RyR1, TRPC3, TRPC4, CaM1, and SERCA. (B) MG53 aggregates around the mitochondria of skeletal muscle in the presence of reactive oxygen species. (C) MG53 promotes plasma membrane repair by facilitating vesicle translocation following injury. Golden spheres represent MG53. Created with BioRender.com.
See this image and copyright information in PMC

References

    1. Adesanya T. M. A., Russell M., Park K. H., Zhou X., Sermersheim M. A., Gumpper K., et al. (2019). MG 53 protein protects aortic valve interstitial cells from membrane injury and fibrocalcific remodeling. J. Am. Heart Assoc. 8:e009960. 10.1161/jaha.118.009960 - DOI - PMC - PubMed
    1. Ahn M. K., Lee K. J., Cai C., Huang M., Cho C. H., Ma J., et al. (2016). Mitsugumin 53 regulates extracellular Ca(2+) entry and intracellular Ca(2+) release via Orai1 and RyR1 in skeletal muscle. Sci. Rep. 6:36909. 10.1038/srep36909 - DOI - PMC - PubMed
    1. Alloush J., Weisleder N. (2013). TRIM proteins in therapeutic membrane repair of muscular dystrophy. JAMA Neurol. 70 928–931. 10.1001/jamaneurol.2013.469 - DOI - PMC - PubMed
    1. Bansal D., Miyake K., Vogel S. S., Groh S., Chen C. C., Williamson R., et al. (2003). Defective membrane repair in dysferlin-deficient muscular dystrophy. Nature 423 168–172. 10.1038/nature01573 - DOI - PubMed
    1. Bian Z., Wang Q., Zhou X., Tan T., Park K. H., Kramer H. F., et al. (2019). Sustained elevation of MG53 in the bloodstream increases tissue regenerative capacity without compromising metabolic function. Nat. Commun. 10:4659. 10.1038/s41467-019-12483-0 - DOI - PMC - PubMed

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