Zinc Binding to MG53 Protein Facilitates Repair of Injury to Cell Membranes

• DOI: 10.1074/jbc.m114.620690
• Publication Date: 2015-04-14T01:52:31Z
• Authors: Chuanxi Cai; Peihui Lin; Hua Zhu; Jae-Kyun Ko; Moonsun Hwang; Tao Tan; Zui Pan; Irina Korichneva; Jianjie Ma
• Keywords: 0301 basic medicine; DNA Repair; Amino Acid Motifs; Mice, Transgenic; Cell Line; redox regulation; Mice; 03 medical and health sciences; trafficking; Escherichia coli; Animals; Humans; Muscle, Skeletal; Electrodes; vesicles; Microscopy, Confocal; Cell Membrane; Membrane Proteins; Recombinant Proteins; Protein Structure, Tertiary; 3. Good health; [SDV] Life Sciences [q-bio]; E3 ubiquitin ligase; Mutation; signaling; Carrier Proteins; Oxidation-Reduction; Plasmids; Protein Binding

Zinc is an essential trace element that participates in a wide range of biological functions, including wound healing. Although Zn2+ deficiency has been linked to compromised healing and tissue repair human diseases, the molecular mechanisms underlying Zn2+-mediated remain unknown. Our previous studies established MG53, TRIM (tripartite motif) family protein, component cell membrane machinery. Domain homology analysis revealed MG53 contains two Zn2+-binding motifs. Here, we show binding indispensable assembly Live imaging illustrated entry from extracellular space for translocation MG53-containing vesicles acute injury sites formation patch. The effect on abolished mg53−/− muscle fibers, suggesting functions as potential target during repair. Mutagenesis suggested both RING B-box motifs constitute domains contribute MG53-mediated Overall, this study establishes base interaction with protection against membrane.Background: zinc finger It not known whether contributes repair.Results: Chelation or mutation affects repair.Conclusion: required repair.Significance: This membrane. Background: Results: Conclusion: Significance: