• Chuanxi Cai, Peihui Lin, Hua Zhu, Jae-Kyun Ko, Moonsun Hwang, Tao Tan, Zui Pan, Irina Korichneva, and Jianjie Ma.
• From the Department of Physiology and Biophysics, Rutgers Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, the Center for Cardiovascular Sciences, Albany Medical College, Albany, New York 12208.
• J. Biol. Chem. 2015 May 29; 290 (22): 13830-9.

AbstractZinc is an essential trace element that participates in a wide range of biological functions, including wound healing. Although Zn(2+) deficiency has been linked to compromised wound healing and tissue repair in human diseases, the molecular mechanisms underlying Zn(2+)-mediated tissue repair remain unknown. Our previous studies established that MG53, a TRIM (tripartite motif) family protein, is an essential component of the cell membrane repair machinery. Domain homology analysis revealed that MG53 contains two Zn(2+)-binding motifs. Here, we show that Zn(2+) binding to MG53 is indispensable to assembly of the cell membrane repair machinery. Live cell imaging illustrated that Zn(2+) entry from extracellular space is essential for translocation of MG53-containing vesicles to the acute membrane injury sites for formation of a repair patch. The effect of Zn(2+) on membrane repair is abolished in mg53(-/-) muscle fibers, suggesting that MG53 functions as a potential target for Zn(2+) during membrane repair. Mutagenesis studies suggested that both RING and B-box motifs of MG53 constitute Zn(2+)-binding domains that contribute to MG53-mediated membrane repair. Overall, this study establishes a base for Zn(2+) interaction with MG53 in protection against injury to the cell membrane. © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

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