ArticleBiochemistry and biophysics reports2025
Insights into the membrane repair mechanism by the coiled-coil-mediated oligomerization of TRIM72.
Article in Biochemistry and biophysics reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- MG53, a Regenerative Myokine Linking Skeletal Muscle to Cardiac Repair.Biomolecules · 2026Review
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3 authors.
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Abstract
TRIpartite Motif-containing 72 (TRIM72, also known as MG53), a RING-type E3 ubiquitin ligase, is critical for plasma membrane repair. Like other TRIM family proteins, TRIM72 has a conserved architecture comprising RING, B-box, coiled-coil, and C-terminal PRY-SPRY domains. While the coiled-coil domain mediates homo-oligomerization, its specific contribution to the membrane repair machinery remains unclear. In this study, we characterized the structural and dynamic properties of the TRIM72 coiled-coil domain, aiming to elucidate its contribution to membrane association. Small-angle X-ray scattering and molecular dynamics simulations revealed that the coiled-coil domain exhibits significant flexibility, including directional movements perpendicular to the membrane. Cryo-electron microscopy further demonstrated that coiled-coil-mediated oligomerization facilitated the tethering of adjacent liposomes. These findings highlight the role of the coiled-coil domain in supporting higher-order assembly on membranes, providing mechanistic insights into the TRIM72-mediated membrane repair.
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