MG53 nucleates assembly of cell membrane repair machinery
| Autor: | Chuanxi Cai, Jae-Kyun Ko, Noah Weisleder, Xiaoli Zhao, Moonsun Hwang, Angela Thornton, Haruko Masumiya, Jianjie Ma, Marco Brotto, Hiroshi Takeshima, Miyuki Nishi, Pei-Hui Lin, Zui Pan, Shinji Komazaki, Noriyuki Matsuda |
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| Rok vydání: | 2008 |
| Předmět: |
Male
Vesicle fusion Muscle Fibers Skeletal Biophysics Muscle Proteins Biology Membrane Fusion Article Exocytosis Cell Line Cell membrane Mice Sarcolemma medicine Animals Regeneration Calcium Signaling Transport Vesicles Cells Cultured Mice Knockout Vesicle Plasma membrane repair SNAP25 Membrane Proteins Intracellular vesicle Extracellular Fluid Cell Biology Cell biology Oxidative Stress Protein Transport medicine.anatomical_structure Membrane protein Animals Newborn Carrier Proteins |
| Zdroj: | Nature cell biology. 11(1) |
| ISSN: | 1476-4679 |
| Popis: | Dynamic membrane repair and remodelling is an elemental process that maintains cell integrity and mediates efficient cellular function. Here we report that MG53, a muscle-specific tripartite motif family protein (TRIM72), is a component of the sarcolemmal membrane-repair machinery. MG53 interacts with phosphatidylserine to associate with intracellular vesicles that traffic to and fuse with sarcolemmal membranes. Mice null for MG53 show progressive myopathy and reduced exercise capability, associated with defective membrane-repair capacity. Injury of the sarcolemmal membrane leads to entry of the extracellular oxidative environment and MG53 oligomerization, resulting in recruitment of MG53-containing vesicles to the injury site. After vesicle translocation, entry of extracellular Ca(2+) facilitates vesicle fusion to reseal the membrane. Our data indicate that intracellular vesicle translocation and Ca(2+)-dependent membrane fusion are distinct steps involved in the repair of membrane damage and that MG53 may initiate the assembly of the membrane repair machinery in an oxidation-dependent manner. |
| Databáze: | OpenAIRE |
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