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Article Dans Une Revue Journal of Biological Chemistry Année : 2015

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

Chuanxi Cai
  • Fonction : Auteur
Peihui Lin
  • Fonction : Auteur
Hua Zhu
  • Fonction : Auteur
Jae-Kyun Ko
  • Fonction : Auteur
Moonsun Hwang
  • Fonction : Auteur
Tao Tan
  • Fonction : Auteur
Zui Pan
  • Fonction : Auteur
Jianjie Ma
  • Fonction : Auteur


Zinc 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.
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Dates et versions

hal-03811654 , version 1 (12-10-2022)



Chuanxi Cai, Peihui Lin, Hua Zhu, Jae-Kyun Ko, Moonsun Hwang, et al.. Zinc Binding to MG53 Protein Facilitates Repair of Injury to Cell Membranes. Journal of Biological Chemistry, 2015, 290 (22), pp.13830-13839. ⟨10.1074/jbc.M114.620690⟩. ⟨hal-03811654⟩


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