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.
Highlights
More than 70 TRIM family proteins exist
The TRIM and PRY domains of Mitsugumin 53 (MG53) constitute the binding region to sarcoplasmic endoplasmic reticulum calcium ion ATPase 1a (SERCA1a) and the interaction of MG53 and SERCA1a reduces the activity of SERCA1a, which takes up calcium from the cytosol to the sarcoplasmic reticulum (Lee et al, 2012; Ahn et al, 2016)
Much is still unknown regarding the physiologic impact of MG53 in skeletal muscle despite the presence of numerous studies involving the protein
Summary
More than 70 TRIM family proteins exist. They are characterized by the presence of a tripartite motif composed of a RING finger, B-box motifs, and a coiled coil region at their N-terminus. MG53, known as TRIM72, was cloned in 2009 using an immunoproteomic library in an attempt to identify proteins involved in myogenesis, calcium signaling, and striated muscle integrity (Weisleder et al, 2008; Tan et al, 2016). Multiple physiologic functions have been attributed to this protein, which have made it an attractive candidate in translational medicine as a potential therapeutic agent. The protein is primarily expressed in striated muscles. Therapeutic applications of the protein relative to skeletal muscle diseases are discussed
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