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Updated: Jun 27, 2026

Visualization of MG53-mediated Cell Membrane Repair Using in vivo and in vitro Systems
Published on: June 30, 2011
MG53 regulates membrane budding and exocytosis in muscle cells
Chuanxi Cai1, Haruko Masumiya2, Noah Weisleder1
1Departments of Physiology and Biophysics, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Abstract:
Membrane recycling and remodeling contribute to multiple cellular functions, including cell fusion events during myogenesis. We have identified a tripartite motif (TRIM72) family member protein named MG53 and defined its role in mediating the dynamic process of membrane fusion and exocytosis in striated muscle. MG53 is a muscle-specific protein that contains a TRIM motif at the amino terminus and a SPRY motif at the carboxyl terminus. Live cell imaging of green fluorescent protein-MG53 fusion construct in cultured myoblasts showed that although MG53 contains no transmembrane segment it is tightly associated with intracellular vesicles and sarcolemmal membrane. RNA interference-mediated knockdown of MG53 expression impeded myoblast differentiation, whereas overexpression of MG53 enhanced vesicle trafficking to and budding from sarcolemmal membrane. Co-expression studies indicated that MG53 activity is regulated by a functional interaction with caveolin-3. Our data reveal a new function for TRIM family proteins in regulating membrane trafficking and fusion in striated muscles.
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