Work

Insights into the membrane repair mechanism by the coiled-coil-mediated oligomerization of TRIM72

Year: 2025

Type: article

Abstract: TRIM72 (MG53), a RING-type E3 ubiquitin ligase, is essential for plasma membrane repair. Similar to other TRIpartite Motif-containing (TRIM) proteins, TRIM72 features a conserved RING, B-box, and coiled-coil architecture with a C-terminal PRYSPRY domain. While the coiled-coil domain mediated 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 exhibited significant flexibility, including directional movement 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 high-order assembly on membranes, providing mechanistic insights into the TRIM72-mediated membrane repair.

Source: Biochemistry and Biophysics Reports

DOI: 10.1016/j.bbrep.2025.102308

Authors: Si Hoon Park, Georg Kempf, Hyun Kyu Song

Institutions: Korea University, Friedrich Miescher Institute

Language: English

Topic: Lipid Membrane Structure and Behavior

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $2,700

Funders: Friedrich Miescher Institute for Biomedical Research, École Polytechnique Fédérale de Lausanne, National Research Foundation of Korea